ATOM 1 N LEU A 4 -39.143 18.200 29.380 1.00103.08 A N ANISOU 1 N LEU A 4 15427 11604 12134 -2444 2353 624 A N ATOM 2 CA LEU A 4 -40.510 18.676 29.200 1.00102.92 A C ANISOU 2 CA LEU A 4 15688 11440 11976 -2259 2152 773 A C ATOM 3 C LEU A 4 -41.268 17.759 28.237 1.00108.50 A C ANISOU 3 C LEU A 4 16440 12182 12604 -2162 2146 785 A C ATOM 4 O LEU A 4 -40.949 17.691 27.049 1.00112.04 A O ANISOU 4 O LEU A 4 17032 12646 12893 -2323 2276 730 A O ATOM 5 CB LEU A 4 -40.507 20.120 28.693 1.00 99.39 A C ANISOU 5 CB LEU A 4 15633 10825 11306 -2395 2123 823 A C ATOM 6 CG LEU A 4 -41.636 21.017 29.201 1.00 93.59 A C ANISOU 6 CG LEU A 4 15127 9919 10515 -2200 1882 950 A C ATOM 7 CD1 LEU A 4 -41.816 20.845 30.697 1.00 88.00 A C ANISOU 7 CD1 LEU A 4 14153 9253 10029 -2037 1782 965 A C ATOM 8 CD2 LEU A 4 -41.351 22.473 28.869 1.00 94.47 A C ANISOU 8 CD2 LEU A 4 15596 9853 10446 -2370 1873 980 A C ATOM 9 N ARG A 5 -42.282 17.064 28.761 1.00112.42 A N ANISOU 9 N ARG A 5 16818 12693 13202 -1911 2000 852 A N ATOM 10 CA ARG A 5 -42.942 15.985 28.032 1.00111.84 A C ANISOU 10 CA ARG A 5 16716 12675 13104 -1813 2009 845 A C ATOM 11 C ARG A 5 -44.115 15.423 28.830 1.00109.96 A C ANISOU 11 C ARG A 5 16362 12439 12979 -1541 1823 928 A C ATOM 12 O ARG A 5 -44.021 15.299 30.055 1.00110.56 A O ANISOU 12 O ARG A 5 16218 12551 13240 -1464 1761 948 A O ATOM 13 CB ARG A 5 -41.930 14.878 27.729 1.00112.14 A C ANISOU 13 CB ARG A 5 16477 12860 13271 -1949 2226 703 A C ATOM 14 CG ARG A 5 -41.247 14.332 28.983 1.00111.11 A C ANISOU 14 CG ARG A 5 15976 12818 13422 -1919 2247 655 A C ATOM 15 CD ARG A 5 -39.773 14.038 28.748 1.00112.67 A C ANISOU 15 CD ARG A 5 15974 13130 13707 -2142 2473 476 A C ATOM 16 N GLN A 6 -45.225 15.065 28.159 1.00100.61 A N ANISOU 16 N GLN A 6 15323 11227 11678 -1404 1734 969 A N ATOM 17 CA GLN A 6 -46.362 14.537 28.913 1.00 92.86 A C ANISOU 17 CA GLN A 6 14229 10259 10792 -1160 1565 1032 A C ATOM 18 C GLN A 6 -47.517 14.041 28.041 1.00 84.62 A C ANISOU 18 C GLN A 6 13340 9201 9612 -1027 1493 1050 A C ATOM 19 O GLN A 6 -48.313 14.846 27.544 1.00 85.06 A O ANISOU 19 O GLN A 6 13686 9159 9473 -946 1356 1092 A O ATOM 20 CB GLN A 6 -46.876 15.605 29.880 1.00 93.69 A C ANISOU 20 CB GLN A 6 14416 10286 10894 -1047 1381 1099 A C ATOM 21 N PRO A 7 -47.643 12.727 27.844 1.00 77.27 A N ANISOU 21 N PRO A 7 12227 8353 8779 -996 1575 1013 A N ATOM 22 CA PRO A 7 -48.722 12.189 26.998 1.00 72.50 A C ANISOU 22 CA PRO A 7 11767 7740 8038 -877 1521 1020 A C ATOM 23 C PRO A 7 -50.113 12.416 27.583 1.00 67.00 A C ANISOU 23 C PRO A 7 11131 7014 7313 -630 1283 1088 A C ATOM 24 O PRO A 7 -50.288 12.533 28.798 1.00 69.60 A O ANISOU 24 O PRO A 7 11293 7364 7788 -543 1188 1123 A O ATOM 25 CB PRO A 7 -48.405 10.692 26.911 1.00 70.51 A C ANISOU 25 CB PRO A 7 11255 7576 7959 -913 1684 954 A C ATOM 26 CG PRO A 7 -47.453 10.401 28.010 1.00 72.05 A C ANISOU 26 CG PRO A 7 11138 7820 8418 -974 1747 934 A C ATOM 27 CD PRO A 7 -46.880 11.680 28.544 1.00 75.63 A C ANISOU 27 CD PRO A 7 11664 8238 8834 -1044 1694 964 A C ATOM 28 N GLN A 8 -51.110 12.469 26.694 1.00 63.17 A N ANISOU 28 N GLN A 8 10885 6492 6625 -518 1184 1093 A N ATOM 29 CA GLN A 8 -52.510 12.655 27.066 1.00 59.42 A C ANISOU 29 CA GLN A 8 10481 6003 6093 -267 952 1120 A C ATOM 30 C GLN A 8 -53.257 11.321 27.164 1.00 56.83 A C ANISOU 30 C GLN A 8 9991 5762 5841 -147 958 1109 A C ATOM 31 O GLN A 8 -52.798 10.280 26.688 1.00 55.63 A O ANISOU 31 O GLN A 8 9734 5651 5751 -251 1140 1079 A O ATOM 32 CB GLN A 8 -53.208 13.562 26.047 1.00 64.87 A C ANISOU 32 CB GLN A 8 11539 6596 6512 -187 802 1118 A C ATOM 33 CG GLN A 8 -54.533 14.135 26.521 1.00 67.83 A C ANISOU 33 CG GLN A 8 12000 6941 6829 81 529 1114 A C ATOM 34 CD GLN A 8 -54.363 15.047 27.716 1.00 69.76 A C ANISOU 34 CD GLN A 8 12174 7145 7186 104 449 1131 A C ATOM 35 NE2 GLN A 8 -54.127 16.330 27.453 1.00 71.43 A N ANISOU 35 NE2 GLN A 8 12636 7220 7286 61 380 1141 A N ATOM 36 OE1 GLN A 8 -54.434 14.605 28.865 1.00 69.27 A O ANISOU 36 OE1 GLN A 8 11850 7170 7300 151 450 1137 A O ATOM 37 N VAL A 9 -54.441 11.376 27.792 1.00 52.26 A N ANISOU 37 N VAL A 9 9393 5209 5254 76 759 1120 A N ATOM 38 CA VAL A 9 -55.217 10.164 28.070 1.00 48.43 A C ANISOU 38 CA VAL A 9 8711 4827 4864 194 741 1100 A C ATOM 39 C VAL A 9 -55.659 9.492 26.774 1.00 53.47 A C ANISOU 39 C VAL A 9 9419 5515 5383 221 758 1010 A C ATOM 40 O VAL A 9 -55.532 8.272 26.610 1.00 52.82 A O ANISOU 40 O VAL A 9 9074 5528 5466 168 862 931 A O ATOM 41 CB VAL A 9 -56.426 10.488 28.968 1.00 43.70 A C ANISOU 41 CB VAL A 9 8027 4306 4273 420 502 1071 A C ATOM 42 CG1 VAL A 9 -56.994 9.216 29.583 1.00 36.55 A C ANISOU 42 CG1 VAL A 9 6726 3584 3579 461 492 997 A C ATOM 43 CG2 VAL A 9 -56.044 11.480 30.051 1.00 49.50 A C ANISOU 43 CG2 VAL A 9 8776 4979 5053 407 456 1137 A C ATOM 44 N ALA A 10 -56.194 10.279 25.836 1.00 54.25 A N ANISOU 44 N ALA A 10 9883 5541 5189 310 638 1016 A N ATOM 45 CA ALA A 10 -56.681 9.706 24.585 1.00 52.61 A C ANISOU 45 CA ALA A 10 9760 5397 4832 347 630 923 A C ATOM 46 C ALA A 10 -55.546 9.044 23.821 1.00 52.00 A C ANISOU 46 C ALA A 10 9643 5327 4786 102 906 897 A C ATOM 47 O ALA A 10 -55.714 7.958 23.253 1.00 51.96 A O ANISOU 47 O ALA A 10 9459 5434 4850 95 971 774 A O ATOM 48 CB ALA A 10 -57.353 10.783 23.734 1.00 53.62 A C ANISOU 48 CB ALA A 10 10334 5425 4615 482 433 956 A C ATOM 49 N GLU A 11 -54.383 9.695 23.791 1.00 55.24 A N ANISOU 49 N GLU A 11 10210 5628 5151 -108 1072 986 A N ATOM 50 CA GLU A 11 -53.221 9.115 23.134 1.00 56.98 A C ANISOU 50 CA GLU A 11 10356 5883 5411 -357 1350 926 A C ATOM 51 C GLU A 11 -52.835 7.797 23.794 1.00 55.43 A C ANISOU 51 C GLU A 11 9683 5792 5585 -376 1455 825 A C ATOM 52 O GLU A 11 -52.531 6.814 23.108 1.00 57.41 A O ANISOU 52 O GLU A 11 9780 6126 5908 -447 1589 691 A O ATOM 53 CB GLU A 11 -52.064 10.113 23.171 1.00 62.17 A C ANISOU 53 CB GLU A 11 11080 6475 6065 -558 1433 953 A C ATOM 54 CG GLU A 11 -50.851 9.726 22.354 1.00 69.68 A C ANISOU 54 CG GLU A 11 11989 7482 7003 -823 1707 862 A C ATOM 55 CD GLU A 11 -49.769 10.786 22.412 1.00 75.37 A C ANISOU 55 CD GLU A 11 12764 8157 7714 -1010 1759 872 A C ATOM 56 OE1 GLU A 11 -48.584 10.443 22.220 1.00 77.45 A O ANISOU 56 OE1 GLU A 11 12873 8489 8066 -1224 1987 780 A O ATOM 57 OE2 GLU A 11 -50.106 11.964 22.660 1.00 77.76 A O1- ANISOU 57 OE2 GLU A 11 13258 8359 7926 -941 1575 954 A O1- ATOM 58 N LEU A 12 -52.843 7.758 25.129 1.00 50.56 A N ANISOU 58 N LEU A 12 8840 5167 5204 -311 1385 883 A N ATOM 59 CA LEU A 12 -52.531 6.518 25.833 1.00 48.11 A C ANISOU 59 CA LEU A 12 8114 4928 5238 -319 1443 817 A C ATOM 60 C LEU A 12 -53.590 5.452 25.573 1.00 47.47 A C ANISOU 60 C LEU A 12 7871 4938 5226 -175 1337 717 A C ATOM 61 O LEU A 12 -53.257 4.286 25.327 1.00 47.08 A O ANISOU 61 O LEU A 12 7588 4929 5373 -224 1434 607 A O ATOM 62 CB LEU A 12 -52.391 6.792 27.330 1.00 44.07 A C ANISOU 62 CB LEU A 12 7437 4395 4911 -285 1368 921 A C ATOM 63 CG LEU A 12 -51.107 7.523 27.724 1.00 43.75 A C ANISOU 63 CG LEU A 12 7440 4284 4901 -458 1507 980 A C ATOM 64 CD1 LEU A 12 -51.085 7.812 29.213 1.00 39.92 A C ANISOU 64 CD1 LEU A 12 6798 3797 4575 -407 1407 1074 A C ATOM 65 CD2 LEU A 12 -49.893 6.702 27.316 1.00 44.96 A C ANISOU 65 CD2 LEU A 12 7391 4465 5226 -627 1728 867 A C ATOM 66 N LEU A 13 -54.871 5.827 25.632 1.00 46.39 A N ANISOU 66 N LEU A 13 7846 4836 4944 4 1131 734 A N ATOM 67 CA LEU A 13 -55.933 4.862 25.358 1.00 44.57 A C ANISOU 67 CA LEU A 13 7461 4710 4763 124 1032 619 A C ATOM 68 C LEU A 13 -55.825 4.312 23.942 1.00 47.19 A C ANISOU 68 C LEU A 13 7872 5073 4986 72 1132 485 A C ATOM 69 O LEU A 13 -56.020 3.112 23.718 1.00 44.38 A O ANISOU 69 O LEU A 13 7286 4777 4800 71 1165 361 A O ATOM 70 CB LEU A 13 -57.302 5.505 25.582 1.00 46.20 A C ANISOU 70 CB LEU A 13 7779 4972 4802 328 792 623 A C ATOM 71 CG LEU A 13 -58.525 4.598 25.417 1.00 47.25 A C ANISOU 71 CG LEU A 13 7731 5242 4980 449 675 485 A C ATOM 72 CD1 LEU A 13 -58.434 3.396 26.346 1.00 44.99 A C ANISOU 72 CD1 LEU A 13 7075 4998 5020 375 729 475 A C ATOM 73 CD2 LEU A 13 -59.806 5.380 25.665 1.00 46.73 A C ANISOU 73 CD2 LEU A 13 7763 5251 4741 659 434 457 A C ATOM 74 N ALA A 14 -55.512 5.175 22.972 1.00 53.33 A N ANISOU 74 N ALA A 14 8984 5807 5471 16 1180 507 A N ATOM 75 CA ALA A 14 -55.367 4.713 21.595 1.00 54.33 A C ANISOU 75 CA ALA A 14 9203 5989 5451 -54 1287 377 A C ATOM 76 C ALA A 14 -54.141 3.822 21.436 1.00 53.64 A C ANISOU 76 C ALA A 14 8881 5912 5586 -242 1534 277 A C ATOM 77 O ALA A 14 -54.195 2.802 20.740 1.00 54.19 A O ANISOU 77 O ALA A 14 8804 6057 5730 -256 1601 106 A O ATOM 78 CB ALA A 14 -55.296 5.909 20.645 1.00 40.18 A C ANISOU 78 CB ALA A 14 7863 4144 3260 -98 1275 451 A C ATOM 79 N GLU A 15 -53.023 4.193 22.068 1.00 52.27 A N ANISOU 79 N GLU A 15 8658 5671 5532 -380 1665 355 A N ATOM 80 CA GLU A 15 -51.836 3.345 22.024 1.00 52.36 A C ANISOU 80 CA GLU A 15 8404 5700 5789 -531 1876 230 A C ATOM 81 C GLU A 15 -52.103 1.993 22.669 1.00 52.10 A C ANISOU 81 C GLU A 15 7997 5676 6122 -433 1813 148 A C ATOM 82 O GLU A 15 -51.647 0.956 22.174 1.00 52.91 A O ANISOU 82 O GLU A 15 7899 5808 6395 -481 1922 -30 A O ATOM 83 CB GLU A 15 -50.659 4.036 22.713 1.00 56.25 A C ANISOU 83 CB GLU A 15 8888 6130 6353 -677 1997 321 A C ATOM 84 CG GLU A 15 -49.447 3.131 22.893 1.00 61.96 A C ANISOU 84 CG GLU A 15 9277 6878 7386 -790 2174 174 A C ATOM 85 CD GLU A 15 -48.381 3.743 23.782 1.00 66.07 A C ANISOU 85 CD GLU A 15 9731 7351 8021 -903 2254 253 A C ATOM 86 OE1 GLU A 15 -48.508 4.935 24.135 1.00 66.27 A O ANISOU 86 OE1 GLU A 15 10003 7319 7857 -928 2203 418 A O ATOM 87 OE2 GLU A 15 -47.416 3.030 24.131 1.00 67.57 A O1- ANISOU 87 OE2 GLU A 15 9619 7557 8498 -957 2354 135 A O1- ATOM 88 N ALA A 16 -52.849 1.986 23.775 1.00 50.34 A N ANISOU 88 N ALA A 16 7684 5423 6018 -305 1634 269 A N ATOM 89 CA ALA A 16 -53.116 0.736 24.471 1.00 49.15 A C ANISOU 89 CA ALA A 16 7216 5261 6198 -244 1566 227 A C ATOM 90 C ALA A 16 -54.019 -0.185 23.662 1.00 50.17 A C ANISOU 90 C ALA A 16 7293 5450 6321 -175 1515 71 A C ATOM 91 O ALA A 16 -53.876 -1.409 23.743 1.00 45.72 A O ANISOU 91 O ALA A 16 6484 4854 6034 -184 1533 -35 A O ATOM 92 CB ALA A 16 -53.744 1.017 25.835 1.00 46.19 A C ANISOU 92 CB ALA A 16 6778 4872 5899 -159 1400 394 A C ATOM 93 N ARG A 17 -54.953 0.367 22.884 1.00 52.94 A N ANISOU 93 N ARG A 17 7871 5876 6368 -99 1435 48 A N ATOM 94 CA ARG A 17 -55.831 -0.509 22.116 1.00 54.50 A C ANISOU 94 CA ARG A 17 8002 6147 6557 -33 1380 -121 A C ATOM 95 C ARG A 17 -55.088 -1.116 20.932 1.00 58.26 A C ANISOU 95 C ARG A 17 8456 6647 7033 -133 1557 -314 A C ATOM 96 O ARG A 17 -55.261 -2.301 20.625 1.00 61.49 A O ANISOU 96 O ARG A 17 8662 7065 7637 -126 1568 -482 A O ATOM 97 CB ARG A 17 -57.074 0.233 21.628 1.00 55.00 A C ANISOU 97 CB ARG A 17 8297 6302 6297 101 1216 -114 A C ATOM 98 CG ARG A 17 -58.067 0.579 22.725 1.00 56.72 A C ANISOU 98 CG ARG A 17 8463 6544 6543 225 1024 -8 A C ATOM 99 CD ARG A 17 -59.384 1.079 22.157 1.00 60.54 A C ANISOU 99 CD ARG A 17 9111 7139 6752 389 839 -75 A C ATOM 100 NE ARG A 17 -59.206 1.810 20.909 1.00 67.69 A N ANISOU 100 NE ARG A 17 10341 8049 7330 398 858 -100 A N ATOM 101 CZ ARG A 17 -59.537 1.306 19.726 1.00 74.34 A C ANISOU 101 CZ ARG A 17 11227 8974 8045 411 869 -266 A C ATOM 102 NH1 ARG A 17 -60.088 0.101 19.673 1.00 77.93 A N1+ ANISOU 102 NH1 ARG A 17 11412 9503 8696 425 856 -430 A N1+ ATOM 103 NH2 ARG A 17 -59.346 2.002 18.611 1.00 76.16 A N ANISOU 103 NH2 ARG A 17 11780 9212 7944 398 885 -268 A N ATOM 104 N ARG A 18 -54.269 -0.312 20.246 1.00 56.51 A N ANISOU 104 N ARG A 18 8446 6442 6585 -241 1698 -306 A N ATOM 105 CA ARG A 18 -53.475 -0.827 19.134 1.00 57.64 A C ANISOU 105 CA ARG A 18 8554 6642 6703 -364 1894 -512 A C ATOM 106 C ARG A 18 -52.620 -2.002 19.580 1.00 57.95 A C ANISOU 106 C ARG A 18 8234 6621 7163 -409 1990 -643 A C ATOM 107 O ARG A 18 -52.546 -3.031 18.896 1.00 61.36 A O ANISOU 107 O ARG A 18 8505 7087 7721 -416 2049 -871 A O ATOM 108 CB ARG A 18 -52.595 0.285 18.561 1.00 59.08 A C ANISOU 108 CB ARG A 18 9006 6850 6592 -524 2053 -456 A C ATOM 109 N ALA A 19 -51.959 -1.864 20.729 1.00 53.80 A N ANISOU 109 N ALA A 19 7583 5998 6862 -429 1989 -511 A N ATOM 110 CA ALA A 19 -51.156 -2.964 21.245 1.00 49.94 A C ANISOU 110 CA ALA A 19 6765 5427 6784 -441 2033 -621 A C ATOM 111 C ALA A 19 -52.038 -4.153 21.602 1.00 46.60 A C ANISOU 111 C ALA A 19 6160 4936 6612 -328 1876 -662 A C ATOM 112 O ALA A 19 -51.681 -5.305 21.329 1.00 47.47 A O ANISOU 112 O ALA A 19 6054 4993 6989 -325 1909 -857 A O ATOM 113 CB ALA A 19 -50.349 -2.502 22.456 1.00 43.83 A C ANISOU 113 CB ALA A 19 5914 4570 6168 -471 2031 -454 A C ATOM 114 N PHE A 20 -53.200 -3.892 22.204 1.00 42.96 A N ANISOU 114 N PHE A 20 5778 4474 6069 -243 1703 -498 A N ATOM 115 CA PHE A 20 -54.112 -4.980 22.540 1.00 44.96 A C ANISOU 115 CA PHE A 20 5872 4679 6532 -176 1566 -535 A C ATOM 116 C PHE A 20 -54.634 -5.671 21.285 1.00 44.23 A C ANISOU 116 C PHE A 20 5773 4657 6375 -161 1594 -780 A C ATOM 117 O PHE A 20 -54.772 -6.900 21.253 1.00 42.93 A O ANISOU 117 O PHE A 20 5416 4413 6483 -154 1562 -917 A O ATOM 118 CB PHE A 20 -55.267 -4.450 23.388 1.00 45.66 A C ANISOU 118 CB PHE A 20 6039 4805 6503 -110 1398 -343 A C ATOM 119 CG PHE A 20 -56.184 -5.522 23.900 1.00 50.04 A C ANISOU 119 CG PHE A 20 6425 5321 7267 -88 1271 -361 A C ATOM 120 CD1 PHE A 20 -57.192 -6.036 23.099 1.00 52.56 A C ANISOU 120 CD1 PHE A 20 6741 5720 7508 -54 1225 -528 A C ATOM 121 CD2 PHE A 20 -56.032 -6.023 25.182 1.00 50.23 A C ANISOU 121 CD2 PHE A 20 6300 5229 7554 -120 1197 -212 A C ATOM 122 CE1 PHE A 20 -58.035 -7.022 23.572 1.00 53.04 A C ANISOU 122 CE1 PHE A 20 6647 5745 7760 -70 1121 -552 A C ATOM 123 CE2 PHE A 20 -56.871 -7.009 25.659 1.00 51.98 A C ANISOU 123 CE2 PHE A 20 6393 5408 7950 -142 1090 -214 A C ATOM 124 CZ PHE A 20 -57.874 -7.509 24.854 1.00 53.90 A C ANISOU 124 CZ PHE A 20 6628 5729 8123 -126 1059 -388 A C ATOM 125 N ARG A 21 -54.934 -4.898 20.240 1.00 43.29 A N ANISOU 125 N ARG A 21 5878 4679 5891 -159 1641 -838 A N ATOM 126 CA ARG A 21 -55.406 -5.491 18.994 1.00 42.91 A C ANISOU 126 CA ARG A 21 5835 4725 5743 -148 1668 -1082 A C ATOM 127 C ARG A 21 -54.326 -6.361 18.362 1.00 51.27 A C ANISOU 127 C ARG A 21 6720 5753 7008 -225 1834 -1321 A C ATOM 128 O ARG A 21 -54.572 -7.522 18.010 1.00 56.00 A O ANISOU 128 O ARG A 21 7142 6318 7818 -205 1814 -1526 A O ATOM 129 CB ARG A 21 -55.855 -4.396 18.027 1.00 43.73 A C ANISOU 129 CB ARG A 21 6251 4982 5381 -132 1670 -1070 A C ATOM 130 N GLU A 22 -53.118 -5.812 18.207 1.00 52.20 A N ANISOU 130 N GLU A 22 6875 5887 7072 -320 1999 -1323 A N ATOM 131 CA GLU A 22 -52.022 -6.573 17.618 1.00 58.35 A C ANISOU 131 CA GLU A 22 7459 6669 8044 -392 2166 -1590 A C ATOM 132 C GLU A 22 -51.749 -7.863 18.383 1.00 61.46 A C ANISOU 132 C GLU A 22 7543 6874 8933 -329 2086 -1667 A C ATOM 133 O GLU A 22 -51.330 -8.860 17.784 1.00 66.48 A O ANISOU 133 O GLU A 22 7990 7490 9778 -329 2148 -1950 A O ATOM 134 CB GLU A 22 -50.758 -5.713 17.565 1.00 57.19 A C ANISOU 134 CB GLU A 22 7373 6576 7781 -521 2352 -1564 A C ATOM 135 N GLU A 23 -51.976 -7.865 19.697 1.00 61.88 A N ANISOU 135 N GLU A 23 7551 6784 9175 -278 1939 -1423 A N ATOM 136 CA GLU A 23 -51.604 -8.996 20.540 1.00 61.39 A C ANISOU 136 CA GLU A 23 7241 6515 9570 -230 1844 -1444 A C ATOM 137 C GLU A 23 -52.712 -10.029 20.691 1.00 56.76 A C ANISOU 137 C GLU A 23 6588 5826 9153 -179 1685 -1467 A C ATOM 138 O GLU A 23 -52.417 -11.224 20.813 1.00 55.39 A O ANISOU 138 O GLU A 23 6224 5481 9343 -151 1632 -1607 A O ATOM 139 CB GLU A 23 -51.192 -8.499 21.932 1.00 63.93 A C ANISOU 139 CB GLU A 23 7553 6738 10000 -225 1768 -1162 A C ATOM 140 CG GLU A 23 -50.900 -9.609 22.938 1.00 65.93 A C ANISOU 140 CG GLU A 23 7598 6758 10694 -173 1624 -1121 A C ATOM 141 CD GLU A 23 -49.520 -10.214 22.762 1.00 67.87 A C ANISOU 141 CD GLU A 23 7631 6919 11236 -152 1697 -1343 A C ATOM 142 OE1 GLU A 23 -48.750 -9.701 21.922 1.00 69.63 A O ANISOU 142 OE1 GLU A 23 7853 7295 11310 -205 1886 -1526 A O ATOM 143 OE2 GLU A 23 -49.203 -11.201 23.462 1.00 67.79 A O1- ANISOU 143 OE2 GLU A 23 7460 6692 11605 -87 1558 -1343 A O1- ATOM 144 N PHE A 24 -53.978 -9.605 20.675 1.00 54.64 A N ANISOU 144 N PHE A 24 6469 5655 8636 -167 1600 -1352 A N ATOM 145 CA PHE A 24 -55.086 -10.496 20.981 1.00 53.21 A C ANISOU 145 CA PHE A 24 6219 5396 8604 -150 1452 -1353 A C ATOM 146 C PHE A 24 -56.118 -10.627 19.868 1.00 50.11 A C ANISOU 146 C PHE A 24 5890 5158 7992 -136 1450 -1546 A C ATOM 147 O PHE A 24 -57.011 -11.476 19.979 1.00 44.67 A O ANISOU 147 O PHE A 24 5117 4414 7442 -142 1346 -1605 A O ATOM 148 CB PHE A 24 -55.769 -10.035 22.277 1.00 51.18 A C ANISOU 148 CB PHE A 24 6016 5117 8313 -154 1318 -1046 A C ATOM 149 CG PHE A 24 -54.868 -10.113 23.476 1.00 54.47 A C ANISOU 149 CG PHE A 24 6350 5367 8978 -169 1284 -857 A C ATOM 150 CD1 PHE A 24 -54.525 -11.336 24.026 1.00 57.09 A C ANISOU 150 CD1 PHE A 24 6522 5468 9703 -180 1200 -874 A C ATOM 151 CD2 PHE A 24 -54.321 -8.964 24.023 1.00 53.63 A C ANISOU 151 CD2 PHE A 24 6339 5326 8713 -168 1323 -671 A C ATOM 152 CE1 PHE A 24 -53.681 -11.409 25.118 1.00 55.02 A C ANISOU 152 CE1 PHE A 24 6196 5054 9656 -178 1142 -700 A C ATOM 153 CE2 PHE A 24 -53.474 -9.032 25.112 1.00 52.91 A C ANISOU 153 CE2 PHE A 24 6163 5099 8841 -177 1283 -513 A C ATOM 154 CZ PHE A 24 -53.156 -10.255 25.660 1.00 52.03 A C ANISOU 154 CZ PHE A 24 5891 4770 9106 -175 1186 -525 A C ATOM 155 N GLY A 25 -56.034 -9.817 18.812 1.00 50.74 A N ANISOU 155 N GLY A 25 6125 5430 7725 -130 1556 -1643 A N ATOM 156 CA GLY A 25 -56.853 -9.994 17.632 1.00 52.52 A C ANISOU 156 CA GLY A 25 6406 5811 7737 -109 1556 -1860 A C ATOM 157 C GLY A 25 -58.213 -9.334 17.664 1.00 51.91 A C ANISOU 157 C GLY A 25 6478 5879 7367 -50 1422 -1756 A C ATOM 158 O GLY A 25 -58.888 -9.299 16.627 1.00 54.51 A O ANISOU 158 O GLY A 25 6884 6366 7460 -16 1407 -1930 A O ATOM 159 N ALA A 26 -58.645 -8.816 18.808 1.00 49.32 A N ANISOU 159 N ALA A 26 6180 5517 7042 -30 1316 -1501 A N ATOM 160 CA ALA A 26 -59.941 -8.169 18.918 1.00 52.13 A C ANISOU 160 CA ALA A 26 6644 6023 7140 43 1176 -1433 A C ATOM 161 C ALA A 26 -59.774 -6.813 19.586 1.00 53.82 A C ANISOU 161 C ALA A 26 7036 6267 7147 83 1147 -1175 A C ATOM 162 O ALA A 26 -58.693 -6.453 20.060 1.00 54.66 A O ANISOU 162 O ALA A 26 7165 6273 7333 35 1237 -1038 A O ATOM 163 CB ALA A 26 -60.931 -9.036 19.708 1.00 48.48 A C ANISOU 163 CB ALA A 26 5997 5519 6904 15 1053 -1434 A C ATOM 164 N GLU A 27 -60.861 -6.061 19.618 1.00 53.87 A N ANISOU 164 N GLU A 27 7159 6415 6895 179 1011 -1132 A N ATOM 165 CA GLU A 27 -60.848 -4.814 20.363 1.00 51.23 A C ANISOU 165 CA GLU A 27 6977 6094 6395 232 952 -903 A C ATOM 166 C GLU A 27 -61.013 -5.109 21.851 1.00 48.38 A C ANISOU 166 C GLU A 27 6439 5659 6284 188 896 -745 A C ATOM 167 O GLU A 27 -61.805 -5.978 22.228 1.00 48.86 A O ANISOU 167 O GLU A 27 6316 5739 6507 156 829 -816 A O ATOM 168 CB GLU A 27 -61.967 -3.888 19.891 1.00 55.34 A C ANISOU 168 CB GLU A 27 7682 6785 6562 380 796 -936 A C ATOM 169 CG GLU A 27 -61.996 -3.655 18.390 1.00 60.46 A C ANISOU 169 CG GLU A 27 8525 7524 6922 426 815 -1091 A C ATOM 170 N PRO A 28 -60.288 -4.404 22.716 1.00 46.93 A N ANISOU 170 N PRO A 28 6310 5398 6123 168 925 -535 A N ATOM 171 CA PRO A 28 -60.529 -4.555 24.151 1.00 46.32 A C ANISOU 171 CA PRO A 28 6090 5285 6222 127 856 -376 A C ATOM 172 C PRO A 28 -61.921 -4.060 24.503 1.00 46.36 A C ANISOU 172 C PRO A 28 6099 5467 6049 215 702 -392 A C ATOM 173 O PRO A 28 -62.473 -3.168 23.855 1.00 48.40 A O ANISOU 173 O PRO A 28 6527 5844 6020 344 627 -453 A O ATOM 174 CB PRO A 28 -59.435 -3.694 24.791 1.00 44.47 A C ANISOU 174 CB PRO A 28 5951 4965 5983 107 918 -179 A C ATOM 175 CG PRO A 28 -59.106 -2.681 23.748 1.00 44.59 A C ANISOU 175 CG PRO A 28 6217 5020 5703 165 968 -215 A C ATOM 176 CD PRO A 28 -59.260 -3.390 22.429 1.00 45.40 A C ANISOU 176 CD PRO A 28 6320 5162 5768 164 1019 -437 A C ATOM 177 N GLU A 29 -62.492 -4.661 25.542 1.00 48.57 A N ANISOU 177 N GLU A 29 6190 5768 6498 139 647 -345 A N ATOM 178 CA GLU A 29 -63.842 -4.333 25.970 1.00 49.73 A C ANISOU 178 CA GLU A 29 6275 6115 6506 194 515 -402 A C ATOM 179 C GLU A 29 -63.873 -3.365 27.143 1.00 48.30 A C ANISOU 179 C GLU A 29 6117 5989 6247 222 459 -230 A C ATOM 180 O GLU A 29 -64.876 -2.666 27.325 1.00 49.25 A O ANISOU 180 O GLU A 29 6239 6293 6179 330 340 -302 A O ATOM 181 CB GLU A 29 -64.595 -5.620 26.328 1.00 55.76 A C ANISOU 181 CB GLU A 29 6807 6908 7470 55 502 -493 A C ATOM 182 CG GLU A 29 -64.670 -6.609 25.161 1.00 61.83 A C ANISOU 182 CG GLU A 29 7538 7629 8326 31 544 -700 A C ATOM 183 CD GLU A 29 -65.394 -7.897 25.507 1.00 67.47 A C ANISOU 183 CD GLU A 29 8042 8341 9252 -132 531 -790 A C ATOM 184 OE1 GLU A 29 -65.817 -8.051 26.671 1.00 69.46 A O ANISOU 184 OE1 GLU A 29 8185 8633 9573 -247 499 -677 A O ATOM 185 OE2 GLU A 29 -65.534 -8.762 24.614 1.00 70.50 A O1- ANISOU 185 OE2 GLU A 29 8376 8683 9727 -160 557 -979 A O1- ATOM 186 N LEU A 30 -62.809 -3.313 27.937 1.00 44.75 A N ANISOU 186 N LEU A 30 5670 5392 5940 139 532 -30 A N ATOM 187 CA LEU A 30 -62.764 -2.502 29.142 1.00 39.37 A C ANISOU 187 CA LEU A 30 4990 4761 5210 143 487 130 A C ATOM 188 C LEU A 30 -61.494 -1.664 29.162 1.00 38.35 A C ANISOU 188 C LEU A 30 5025 4493 5053 171 556 274 A C ATOM 189 O LEU A 30 -60.442 -2.087 28.673 1.00 37.66 A O ANISOU 189 O LEU A 30 4967 4249 5093 116 665 293 A O ATOM 190 CB LEU A 30 -62.842 -3.374 30.393 1.00 35.21 A C ANISOU 190 CB LEU A 30 4263 4222 4892 -30 492 243 A C ATOM 191 CG LEU A 30 -64.053 -4.307 30.410 1.00 39.46 A C ANISOU 191 CG LEU A 30 4632 4889 5473 -118 449 103 A C ATOM 192 CD1 LEU A 30 -63.881 -5.424 31.430 1.00 32.70 A C ANISOU 192 CD1 LEU A 30 3631 3938 4854 -337 475 241 A C ATOM 193 CD2 LEU A 30 -65.312 -3.505 30.694 1.00 32.63 A C ANISOU 193 CD2 LEU A 30 3722 4299 4378 -27 344 -15 A C ATOM 194 N ALA A 31 -61.608 -0.467 29.735 1.00 38.44 A N ANISOU 194 N ALA A 31 5133 4573 4902 254 490 349 A N ATOM 195 CA ALA A 31 -60.496 0.467 29.834 1.00 35.72 A C ANISOU 195 CA ALA A 31 4953 4110 4511 267 548 479 A C ATOM 196 C ALA A 31 -60.522 1.126 31.206 1.00 32.36 A C ANISOU 196 C ALA A 31 4474 3743 4079 260 490 607 A C ATOM 197 O ALA A 31 -61.587 1.321 31.797 1.00 31.61 A O ANISOU 197 O ALA A 31 4290 3817 3903 307 382 554 A O ATOM 198 CB ALA A 31 -60.547 1.529 28.724 1.00 39.23 A C ANISOU 198 CB ALA A 31 5671 4544 4691 400 520 413 A C ATOM 199 N VAL A 32 -59.333 1.465 31.706 1.00 33.57 A N ANISOU 199 N VAL A 32 4665 3775 4315 195 566 751 A N ATOM 200 CA VAL A 32 -59.166 1.941 33.076 1.00 31.22 A C ANISOU 200 CA VAL A 32 4293 3524 4044 161 526 878 A C ATOM 201 C VAL A 32 -57.883 2.755 33.134 1.00 36.12 A C ANISOU 201 C VAL A 32 5048 4011 4665 141 603 979 A C ATOM 202 O VAL A 32 -56.948 2.519 32.363 1.00 40.35 A O ANISOU 202 O VAL A 32 5646 4416 5267 92 716 971 A O ATOM 203 CB VAL A 32 -59.139 0.760 34.080 1.00 29.06 A C ANISOU 203 CB VAL A 32 3786 3266 3988 17 532 966 A C ATOM 204 CG1 VAL A 32 -57.784 0.677 34.770 1.00 29.47 A C ANISOU 204 CG1 VAL A 32 3805 3185 4207 -71 595 1122 A C ATOM 205 CG2 VAL A 32 -60.271 0.888 35.094 1.00 29.63 A C ANISOU 205 CG2 VAL A 32 3735 3550 3973 7 432 956 A C ATOM 206 N SER A 33 -57.839 3.721 34.054 1.00 36.17 A N ANISOU 206 N SER A 33 5084 4065 4594 167 547 1050 A N ATOM 207 CA SER A 33 -56.646 4.534 34.244 1.00 38.32 A C ANISOU 207 CA SER A 33 5467 4221 4870 128 617 1138 A C ATOM 208 C SER A 33 -56.417 4.802 35.727 1.00 38.89 A C ANISOU 208 C SER A 33 5410 4361 5006 82 573 1244 A C ATOM 209 O SER A 33 -57.358 4.829 36.526 1.00 39.44 A O ANISOU 209 O SER A 33 5375 4589 5022 114 472 1231 A O ATOM 210 CB SER A 33 -56.742 5.866 33.480 1.00 39.28 A C ANISOU 210 CB SER A 33 5878 4289 4759 228 590 1093 A C ATOM 211 OG SER A 33 -57.839 6.645 33.923 1.00 44.72 A O ANISOU 211 OG SER A 33 6609 5092 5293 366 431 1041 A O ATOM 212 N ALA A 34 -55.145 5.013 36.080 1.00 36.76 A N ANISOU 212 N ALA A 34 5136 3991 4839 -2 654 1330 A N ATOM 213 CA ALA A 34 -54.702 5.290 37.445 1.00 35.57 A C ANISOU 213 CA ALA A 34 4872 3894 4751 -55 620 1431 A C ATOM 214 C ALA A 34 -53.420 6.111 37.378 1.00 34.88 A C ANISOU 214 C ALA A 34 4886 3689 4678 -104 708 1460 A C ATOM 215 O ALA A 34 -52.500 5.739 36.633 1.00 35.73 A O ANISOU 215 O ALA A 34 5009 3682 4886 -168 825 1439 A O ATOM 216 CB ALA A 34 -54.462 4.012 38.248 1.00 35.57 A C ANISOU 216 CB ALA A 34 4642 3916 4955 -150 608 1523 A C ATOM 217 N PRO A 35 -53.324 7.207 38.125 1.00 31.39 A N ANISOU 217 N PRO A 35 4501 3282 4143 -88 661 1484 A N ATOM 218 CA PRO A 35 -52.183 8.116 37.984 1.00 31.97 A C ANISOU 218 CA PRO A 35 4695 3246 4205 -153 742 1481 A C ATOM 219 C PRO A 35 -50.989 7.746 38.855 1.00 36.45 A C ANISOU 219 C PRO A 35 5065 3842 4942 -259 755 1488 A C ATOM 220 O PRO A 35 -51.084 6.970 39.809 1.00 39.47 A O ANISOU 220 O PRO A 35 5251 4315 5430 -267 687 1539 A O ATOM 221 CB PRO A 35 -52.773 9.462 38.427 1.00 30.22 A C ANISOU 221 CB PRO A 35 4628 3052 3804 -67 647 1468 A C ATOM 222 CG PRO A 35 -53.764 9.074 39.477 1.00 32.01 A C ANISOU 222 CG PRO A 35 4666 3470 4027 -7 521 1473 A C ATOM 223 CD PRO A 35 -54.360 7.756 39.018 1.00 32.74 A C ANISOU 223 CD PRO A 35 4642 3609 4190 -7 526 1469 A C ATOM 224 N GLY A 36 -49.845 8.323 38.493 1.00 38.16 A N ANISOU 224 N GLY A 36 5349 3981 5171 -344 842 1435 A N ATOM 225 CA GLY A 36 -48.692 8.379 39.366 1.00 36.96 A C ANISOU 225 CA GLY A 36 5050 3852 5140 -423 858 1438 A C ATOM 226 C GLY A 36 -48.857 9.460 40.417 1.00 38.83 A C ANISOU 226 C GLY A 36 5325 4142 5288 -412 788 1478 A C ATOM 227 O GLY A 36 -49.900 10.105 40.535 1.00 41.92 A O ANISOU 227 O GLY A 36 5837 4553 5537 -329 720 1506 A O ATOM 228 N ARG A 37 -47.799 9.657 41.201 1.00 40.85 A N ANISOU 228 N ARG A 37 5461 4418 5641 -487 809 1482 A N ATOM 229 CA ARG A 37 -47.895 10.576 42.323 1.00 42.54 A C ANISOU 229 CA ARG A 37 5671 4695 5800 -483 748 1529 A C ATOM 230 C ARG A 37 -46.563 11.268 42.579 1.00 41.54 A C ANISOU 230 C ARG A 37 5523 4522 5738 -601 832 1491 A C ATOM 231 O ARG A 37 -45.492 10.726 42.290 1.00 39.74 A O ANISOU 231 O ARG A 37 5180 4271 5650 -677 914 1445 A O ATOM 232 CB ARG A 37 -48.371 9.828 43.577 1.00 43.91 A C ANISOU 232 CB ARG A 37 5630 5028 6026 -439 626 1617 A C ATOM 233 CG ARG A 37 -47.977 10.459 44.893 1.00 48.13 A C ANISOU 233 CG ARG A 37 6061 5664 6564 -477 574 1674 A C ATOM 234 CD ARG A 37 -46.958 9.586 45.608 1.00 45.77 A C ANISOU 234 CD ARG A 37 5539 5413 6439 -528 545 1714 A C ATOM 235 NE ARG A 37 -45.623 9.740 45.039 1.00 46.11 A N ANISOU 235 NE ARG A 37 5568 5342 6611 -604 664 1642 A N ATOM 236 CZ ARG A 37 -44.571 8.999 45.370 1.00 45.41 A C ANISOU 236 CZ ARG A 37 5281 5255 6718 -639 659 1663 A C ATOM 237 NH1 ARG A 37 -43.397 9.228 44.798 1.00 43.27 A N1+ ANISOU 237 NH1 ARG A 37 4974 4901 6564 -723 791 1568 A N1+ ATOM 238 NH2 ARG A 37 -44.688 8.027 46.265 1.00 46.74 A N ANISOU 238 NH2 ARG A 37 5286 5505 6967 -600 521 1779 A N ATOM 239 N VAL A 38 -46.653 12.485 43.117 1.00 40.68 A N ANISOU 239 N VAL A 38 5518 4398 5540 -615 819 1507 A N ATOM 240 CA VAL A 38 -45.521 13.215 43.679 1.00 38.20 A C ANISOU 240 CA VAL A 38 5154 4067 5294 -735 884 1483 A C ATOM 241 C VAL A 38 -45.921 13.711 45.062 1.00 37.44 A C ANISOU 241 C VAL A 38 4967 4114 5146 -681 743 1498 A C ATOM 242 O VAL A 38 -47.011 14.268 45.233 1.00 40.50 A O ANISOU 242 O VAL A 38 5475 4529 5386 -578 646 1485 A O ATOM 243 CB VAL A 38 -45.089 14.394 42.784 1.00 38.53 A C ANISOU 243 CB VAL A 38 5466 3945 5229 -839 986 1393 A C ATOM 244 CG1 VAL A 38 -46.153 15.487 42.782 1.00 37.68 A C ANISOU 244 CG1 VAL A 38 5627 3751 4940 -745 903 1406 A C ATOM 245 CG2 VAL A 38 -43.753 14.952 43.254 1.00 40.94 A C ANISOU 245 CG2 VAL A 38 5681 4244 5631 -1003 1083 1330 A C ATOM 246 N ASN A 39 -45.048 13.506 46.045 1.00 36.56 A N ANISOU 246 N ASN A 39 4632 4111 5149 -741 720 1500 A N ATOM 247 CA ASN A 39 -45.296 13.962 47.407 1.00 36.22 A C ANISOU 247 CA ASN A 39 4485 4233 5046 -711 591 1499 A C ATOM 248 C ASN A 39 -44.700 15.351 47.603 1.00 35.00 A C ANISOU 248 C ASN A 39 4437 4011 4850 -791 632 1386 A C ATOM 249 O ASN A 39 -43.478 15.519 47.548 1.00 33.12 A O ANISOU 249 O ASN A 39 4131 3729 4722 -918 726 1330 A O ATOM 250 CB ASN A 39 -44.718 12.987 48.430 1.00 37.25 A C ANISOU 250 CB ASN A 39 4331 4523 5298 -727 513 1573 A C ATOM 251 CG ASN A 39 -45.183 13.288 49.840 1.00 42.72 A C ANISOU 251 CG ASN A 39 4919 5429 5885 -697 371 1591 A C ATOM 252 ND2 ASN A 39 -44.569 12.636 50.823 1.00 46.78 A N ANISOU 252 ND2 ASN A 39 5218 6081 6477 -726 287 1657 A N ATOM 253 OD1 ASN A 39 -46.109 14.076 50.042 1.00 45.31 A O ANISOU 253 OD1 ASN A 39 5357 5803 6056 -642 327 1536 A O ATOM 254 N LEU A 40 -45.558 16.341 47.847 1.00 33.32 A N ANISOU 254 N LEU A 40 4380 3792 4487 -719 554 1331 A N ATOM 255 CA LEU A 40 -45.064 17.695 48.063 1.00 35.80 A C ANISOU 255 CA LEU A 40 4821 4013 4767 -793 573 1218 A C ATOM 256 C LEU A 40 -44.247 17.786 49.343 1.00 36.76 A C ANISOU 256 C LEU A 40 4698 4309 4961 -863 533 1175 A C ATOM 257 O LEU A 40 -43.201 18.439 49.381 1.00 32.20 A O ANISOU 257 O LEU A 40 4126 3659 4449 -1000 613 1091 A O ATOM 258 CB LEU A 40 -46.233 18.677 48.098 1.00 33.82 A C ANISOU 258 CB LEU A 40 4780 3713 4358 -661 461 1149 A C ATOM 259 CG LEU A 40 -47.123 18.669 46.853 1.00 39.87 A C ANISOU 259 CG LEU A 40 5804 4312 5034 -564 463 1179 A C ATOM 260 CD1 LEU A 40 -48.200 19.738 46.949 1.00 30.61 A C ANISOU 260 CD1 LEU A 40 4829 3080 3721 -408 318 1078 A C ATOM 261 CD2 LEU A 40 -46.289 18.832 45.593 1.00 36.82 A C ANISOU 261 CD2 LEU A 40 5627 3684 4680 -708 627 1206 A C ATOM 262 N ILE A 41 -44.706 17.120 50.413 1.00 37.18 A N ANISOU 262 N ILE A 41 4533 4604 4990 -786 408 1230 A N ATOM 263 CA ILE A 41 -43.978 17.097 51.674 1.00 37.77 A C ANISOU 263 CA ILE A 41 4371 4870 5109 -842 344 1206 A C ATOM 264 C ILE A 41 -44.579 16.007 52.544 1.00 40.86 A C ANISOU 264 C ILE A 41 4567 5500 5456 -774 221 1329 A C ATOM 265 O ILE A 41 -45.743 15.629 52.366 1.00 39.33 A O ANISOU 265 O ILE A 41 4430 5351 5164 -687 179 1384 A O ATOM 266 CB ILE A 41 -44.040 18.486 52.365 1.00 39.80 A C ANISOU 266 CB ILE A 41 4692 5152 5277 -854 296 1052 A C ATOM 267 CG1 ILE A 41 -43.028 18.558 53.511 1.00 42.26 A C ANISOU 267 CG1 ILE A 41 4768 5639 5650 -941 255 1001 A C ATOM 268 CG2 ILE A 41 -45.446 18.762 52.870 1.00 38.21 A C ANISOU 268 CG2 ILE A 41 4528 5083 4908 -715 172 1020 A C ATOM 269 CD1 ILE A 41 -42.908 19.934 54.139 1.00 41.03 A C ANISOU 269 CD1 ILE A 41 4666 5489 5435 -976 223 823 A C ATOM 270 N GLY A 42 -43.787 15.498 53.485 1.00 43.80 A N ANISOU 270 N GLY A 42 4718 6029 5895 -823 157 1371 A N ATOM 271 CA GLY A 42 -44.247 14.445 54.367 1.00 42.46 A C ANISOU 271 CA GLY A 42 4392 6072 5670 -792 29 1516 A C ATOM 272 C GLY A 42 -43.641 13.105 54.006 1.00 45.45 A C ANISOU 272 C GLY A 42 4676 6380 6215 -797 24 1656 A C ATOM 273 O GLY A 42 -44.356 12.109 53.866 1.00 46.59 A O ANISOU 273 O GLY A 42 4825 6537 6338 -760 -18 1793 A O ATOM 274 N GLU A 43 -42.320 13.070 53.850 1.00 44.53 A N ANISOU 274 N GLU A 43 4462 6185 6270 -843 62 1600 A N ATOM 275 CA GLU A 43 -41.631 11.890 53.352 1.00 43.57 A C ANISOU 275 CA GLU A 43 4246 5964 6343 -827 61 1677 A C ATOM 276 C GLU A 43 -41.306 10.934 54.492 1.00 44.62 A C ANISOU 276 C GLU A 43 4197 6252 6506 -800 -132 1811 A C ATOM 277 O GLU A 43 -40.914 11.359 55.583 1.00 46.49 A O ANISOU 277 O GLU A 43 4325 6662 6678 -826 -230 1783 A O ATOM 278 CB GLU A 43 -40.346 12.299 52.630 1.00 44.07 A C ANISOU 278 CB GLU A 43 4266 5897 6580 -892 194 1516 A C ATOM 279 CG GLU A 43 -40.112 11.609 51.299 1.00 45.23 A C ANISOU 279 CG GLU A 43 4457 5855 6874 -884 315 1506 A C ATOM 280 CD GLU A 43 -41.239 11.849 50.312 1.00 48.27 A C ANISOU 280 CD GLU A 43 5087 6117 7137 -867 416 1536 A C ATOM 281 OE1 GLU A 43 -42.263 11.137 50.394 1.00 46.78 A O ANISOU 281 OE1 GLU A 43 4937 5957 6880 -790 335 1671 A O ATOM 282 OE2 GLU A 43 -41.109 12.757 49.461 1.00 50.02 A O1- ANISOU 282 OE2 GLU A 43 5468 6215 7321 -938 569 1424 A O1- ATOM 283 N HIS A 44 -41.480 9.636 54.229 1.00 47.60 A N ANISOU 283 N HIS A 44 4556 6556 6976 -750 -198 1960 A N ATOM 284 CA HIS A 44 -41.164 8.582 55.197 1.00 47.01 A C ANISOU 284 CA HIS A 44 4353 6567 6941 -720 -406 2121 A C ATOM 285 C HIS A 44 -41.871 8.801 56.530 1.00 46.02 A C ANISOU 285 C HIS A 44 4227 6691 6568 -764 -534 2226 A C ATOM 286 O HIS A 44 -41.370 8.419 57.590 1.00 50.62 A O ANISOU 286 O HIS A 44 4700 7403 7130 -767 -710 2314 A O ATOM 287 CB HIS A 44 -39.653 8.442 55.392 1.00 51.01 A C ANISOU 287 CB HIS A 44 4673 7054 7655 -691 -472 2025 A C ATOM 288 CG HIS A 44 -38.957 7.793 54.235 1.00 56.78 A C ANISOU 288 CG HIS A 44 5358 7573 8643 -640 -393 1944 A C ATOM 289 CD2 HIS A 44 -38.323 8.320 53.161 1.00 58.26 A C ANISOU 289 CD2 HIS A 44 5534 7648 8953 -674 -195 1740 A C ATOM 290 ND1 HIS A 44 -38.879 6.424 54.091 1.00 58.88 A N ANISOU 290 ND1 HIS A 44 5588 7723 9061 -554 -522 2071 A N ATOM 291 CE1 HIS A 44 -38.218 6.136 52.985 1.00 59.83 A C ANISOU 291 CE1 HIS A 44 5652 7682 9398 -519 -409 1923 A C ATOM 292 NE2 HIS A 44 -37.870 7.269 52.401 1.00 59.62 A N ANISOU 292 NE2 HIS A 44 5638 7669 9346 -604 -201 1724 A N ATOM 293 N THR A 45 -43.044 9.431 56.486 1.00 43.39 A N ANISOU 293 N THR A 45 4010 6441 6035 -797 -453 2201 A N ATOM 294 CA THR A 45 -43.904 9.533 57.653 1.00 46.53 A C ANISOU 294 CA THR A 45 4401 7101 6179 -853 -550 2283 A C ATOM 295 C THR A 45 -45.129 8.639 57.581 1.00 46.02 A C ANISOU 295 C THR A 45 4418 7064 6002 -884 -570 2446 A C ATOM 296 O THR A 45 -45.760 8.403 58.616 1.00 47.81 A O ANISOU 296 O THR A 45 4622 7523 6022 -963 -664 2551 A O ATOM 297 CB THR A 45 -44.368 10.982 57.853 1.00 46.00 A C ANISOU 297 CB THR A 45 4366 7160 5951 -867 -465 2086 A C ATOM 298 CG2 THR A 45 -43.176 11.890 58.095 1.00 46.50 A C ANISOU 298 CG2 THR A 45 4346 7219 6104 -872 -453 1924 A C ATOM 299 OG1 THR A 45 -45.075 11.422 56.687 1.00 45.53 A O ANISOU 299 OG1 THR A 45 4453 6942 5905 -823 -319 1991 A O ATOM 300 N ASP A 46 -45.476 8.133 56.397 1.00 44.83 A N ANISOU 300 N ASP A 46 4357 6701 5974 -842 -477 2459 A N ATOM 301 CA ASP A 46 -46.744 7.427 56.245 1.00 44.90 A C ANISOU 301 CA ASP A 46 4442 6748 5871 -883 -472 2569 A C ATOM 302 C ASP A 46 -46.761 6.115 57.025 1.00 47.40 A C ANISOU 302 C ASP A 46 4735 7105 6171 -958 -632 2810 A C ATOM 303 O ASP A 46 -47.731 5.823 57.734 1.00 51.64 A O ANISOU 303 O ASP A 46 5286 7823 6514 -1039 -670 2815 A O ATOM 304 CB ASP A 46 -47.057 7.214 54.760 1.00 42.60 A C ANISOU 304 CB ASP A 46 4250 6219 5717 -817 -341 2508 A C ATOM 305 CG ASP A 46 -46.083 6.283 54.075 1.00 43.88 A C ANISOU 305 CG ASP A 46 4392 6131 6148 -770 -359 2568 A C ATOM 306 OD1 ASP A 46 -44.925 6.186 54.528 1.00 47.50 A O ANISOU 306 OD1 ASP A 46 4752 6568 6729 -751 -443 2580 A O ATOM 307 OD2 ASP A 46 -46.479 5.653 53.072 1.00 40.97 A O1- ANISOU 307 OD2 ASP A 46 4099 5603 5866 -718 -301 2515 A O1- ATOM 308 N TYR A 47 -45.709 5.303 56.909 1.00 46.58 A N ANISOU 308 N TYR A 47 4596 6816 6287 -911 -732 2914 A N ATOM 309 CA TYR A 47 -45.687 4.080 57.705 1.00 49.27 A C ANISOU 309 CA TYR A 47 4944 7155 6621 -959 -903 3061 A C ATOM 310 C TYR A 47 -45.379 4.337 59.176 1.00 50.88 A C ANISOU 310 C TYR A 47 5088 7602 6641 -1037 -1047 3155 A C ATOM 311 O TYR A 47 -45.369 3.386 59.967 1.00 56.58 A O ANISOU 311 O TYR A 47 5845 8324 7328 -1099 -1180 3263 A O ATOM 312 CB TYR A 47 -44.695 3.082 57.099 1.00 51.48 A C ANISOU 312 CB TYR A 47 5211 7145 7205 -861 -991 3129 A C ATOM 313 CG TYR A 47 -43.280 3.584 56.924 1.00 52.42 A C ANISOU 313 CG TYR A 47 5204 7190 7521 -752 -1026 3063 A C ATOM 314 CD1 TYR A 47 -42.568 4.106 57.996 1.00 55.79 A C ANISOU 314 CD1 TYR A 47 5532 7797 7871 -756 -1144 3051 A C ATOM 315 CD2 TYR A 47 -42.664 3.558 55.679 1.00 51.35 A C ANISOU 315 CD2 TYR A 47 5034 6834 7641 -653 -909 2901 A C ATOM 316 CE1 TYR A 47 -41.277 4.562 57.844 1.00 56.44 A C ANISOU 316 CE1 TYR A 47 5473 7834 8138 -664 -1150 2877 A C ATOM 317 CE2 TYR A 47 -41.373 4.021 55.514 1.00 54.10 A C ANISOU 317 CE2 TYR A 47 5244 7147 8165 -576 -900 2726 A C ATOM 318 CZ TYR A 47 -40.684 4.521 56.602 1.00 56.23 A C ANISOU 318 CZ TYR A 47 5405 7593 8367 -582 -1021 2711 A C ATOM 319 OH TYR A 47 -39.399 4.983 56.442 1.00 55.79 A O ANISOU 319 OH TYR A 47 5189 7520 8489 -519 -1007 2512 A O ATOM 320 N ASN A 48 -45.142 5.592 59.555 1.00 51.92 A N ANISOU 320 N ASN A 48 5145 7931 6652 -1034 -1013 3069 A N ATOM 321 CA ASN A 48 -45.037 6.006 60.946 1.00 52.48 A C ANISOU 321 CA ASN A 48 5152 8295 6494 -1114 -1129 3105 A C ATOM 322 C ASN A 48 -46.321 6.663 61.439 1.00 56.02 A C ANISOU 322 C ASN A 48 5616 9028 6642 -1228 -1028 3021 A C ATOM 323 O ASN A 48 -46.309 7.349 62.467 1.00 58.44 A O ANISOU 323 O ASN A 48 5851 9615 6740 -1286 -1075 2969 A O ATOM 324 CB ASN A 48 -43.842 6.943 61.137 1.00 53.75 A C ANISOU 324 CB ASN A 48 5188 8479 6757 -1029 -1142 2920 A C ATOM 325 CG ASN A 48 -42.518 6.203 61.141 1.00 56.47 A C ANISOU 325 CG ASN A 48 5463 8647 7345 -935 -1304 2994 A C ATOM 326 ND2 ASN A 48 -41.605 6.604 60.261 1.00 53.55 A N ANISOU 326 ND2 ASN A 48 5018 8098 7229 -832 -1212 2802 A N ATOM 327 OD1 ASN A 48 -42.317 5.286 61.938 1.00 58.52 A O ANISOU 327 OD1 ASN A 48 5739 8937 7559 -959 -1516 3211 A O ATOM 328 N GLN A 49 -47.428 6.461 60.723 1.00 53.80 A N ANISOU 328 N GLN A 49 5406 8685 6350 -1244 -895 2950 A N ATOM 329 CA GLN A 49 -48.725 7.028 61.089 1.00 51.44 A C ANISOU 329 CA GLN A 49 5095 8652 5796 -1327 -807 2823 A C ATOM 330 C GLN A 49 -48.703 8.552 61.077 1.00 50.06 A C ANISOU 330 C GLN A 49 4863 8632 5523 -1265 -730 2627 A C ATOM 331 O GLN A 49 -49.366 9.196 61.891 1.00 51.46 A O ANISOU 331 O GLN A 49 4977 9118 5456 -1333 -721 2515 A O ATOM 332 CB GLN A 49 -49.178 6.529 62.464 1.00 51.31 A C ANISOU 332 CB GLN A 49 5048 8882 5567 -1492 -891 2883 A C ATOM 333 CG GLN A 49 -49.366 5.032 62.561 1.00 53.50 A C ANISOU 333 CG GLN A 49 5411 8991 5925 -1566 -965 3027 A C ATOM 334 CD GLN A 49 -50.391 4.636 63.609 1.00 60.44 A C ANISOU 334 CD GLN A 49 6286 10126 6551 -1762 -979 3040 A C ATOM 335 NE2 GLN A 49 -49.918 4.060 64.708 1.00 61.16 A N ANISOU 335 NE2 GLN A 49 6401 10270 6566 -1869 -1106 3188 A N ATOM 336 OE1 GLN A 49 -51.593 4.836 63.429 1.00 66.33 A O ANISOU 336 OE1 GLN A 49 7013 11023 7169 -1819 -882 2916 A O ATOM 337 N GLY A 50 -47.958 9.144 60.156 1.00 48.88 A N ANISOU 337 N GLY A 50 4736 8233 5602 -1128 -662 2492 A N ATOM 338 CA GLY A 50 -47.797 10.582 60.088 1.00 50.54 A C ANISOU 338 CA GLY A 50 4924 8482 5798 -1054 -591 2234 A C ATOM 339 C GLY A 50 -48.715 11.245 59.082 1.00 49.73 A C ANISOU 339 C GLY A 50 4914 8287 5696 -971 -461 2058 A C ATOM 340 O GLY A 50 -49.807 10.751 58.773 1.00 49.48 A O ANISOU 340 O GLY A 50 4918 8302 5580 -991 -428 2092 A O ATOM 341 N LEU A 51 -48.265 12.386 58.564 1.00 48.56 A N ANISOU 341 N LEU A 51 4813 8000 5638 -883 -396 1865 A N ATOM 342 CA LEU A 51 -49.006 13.182 57.598 1.00 47.89 A C ANISOU 342 CA LEU A 51 4851 7789 5555 -782 -304 1691 A C ATOM 343 C LEU A 51 -48.287 13.187 56.255 1.00 45.30 A C ANISOU 343 C LEU A 51 4653 7107 5453 -724 -213 1698 A C ATOM 344 O LEU A 51 -47.056 13.137 56.187 1.00 46.67 A O ANISOU 344 O LEU A 51 4796 7157 5780 -751 -204 1730 A O ATOM 345 CB LEU A 51 -49.174 14.626 58.086 1.00 48.96 A C ANISOU 345 CB LEU A 51 4980 8035 5586 -736 -313 1447 A C ATOM 346 CG LEU A 51 -49.885 14.872 59.417 1.00 47.11 A C ANISOU 346 CG LEU A 51 4602 8186 5111 -789 -388 1363 A C ATOM 347 CD1 LEU A 51 -49.869 16.356 59.752 1.00 44.56 A C ANISOU 347 CD1 LEU A 51 4283 7906 4742 -720 -400 1091 A C ATOM 348 CD2 LEU A 51 -51.316 14.351 59.370 1.00 48.47 A C ANISOU 348 CD2 LEU A 51 4753 8535 5129 -795 -379 1362 A C ATOM 349 N VAL A 52 -49.071 13.251 55.180 1.00 42.95 A N ANISOU 349 N VAL A 52 4489 6667 5163 -648 -146 1651 A N ATOM 350 CA VAL A 52 -48.530 13.347 53.831 1.00 38.60 A C ANISOU 350 CA VAL A 52 4086 5802 4780 -604 -47 1639 A C ATOM 351 C VAL A 52 -49.335 14.376 53.049 1.00 34.94 A C ANISOU 351 C VAL A 52 3801 5233 4241 -500 -11 1474 A C ATOM 352 O VAL A 52 -50.511 14.622 53.336 1.00 36.05 A O ANISOU 352 O VAL A 52 3933 5534 4231 -437 -65 1388 A O ATOM 353 CB VAL A 52 -48.538 11.981 53.112 1.00 40.23 A C ANISOU 353 CB VAL A 52 4291 5892 5100 -618 -19 1803 A C ATOM 354 CG1 VAL A 52 -47.652 10.988 53.848 1.00 39.83 A C ANISOU 354 CG1 VAL A 52 4091 5896 5148 -695 -89 1964 A C ATOM 355 CG2 VAL A 52 -49.960 11.452 52.999 1.00 44.25 A C ANISOU 355 CG2 VAL A 52 4813 6517 5482 -592 -41 1827 A C ATOM 356 N LEU A 53 -48.687 14.985 52.057 1.00 31.83 A N ANISOU 356 N LEU A 53 3574 4572 3949 -487 73 1421 A N ATOM 357 CA LEU A 53 -49.310 15.990 51.196 1.00 30.81 A C ANISOU 357 CA LEU A 53 3672 4278 3755 -388 88 1290 A C ATOM 358 C LEU A 53 -48.951 15.692 49.745 1.00 30.91 A C ANISOU 358 C LEU A 53 3858 4021 3865 -396 197 1348 A C ATOM 359 O LEU A 53 -48.211 16.447 49.103 1.00 29.86 A O ANISOU 359 O LEU A 53 3890 3675 3780 -443 273 1301 A O ATOM 360 CB LEU A 53 -48.874 17.401 51.595 1.00 33.18 A C ANISOU 360 CB LEU A 53 4054 4522 4031 -392 67 1139 A C ATOM 361 CG LEU A 53 -49.678 18.555 50.996 1.00 37.03 A C ANISOU 361 CG LEU A 53 4784 4857 4429 -262 19 988 A C ATOM 362 CD1 LEU A 53 -51.156 18.364 51.298 1.00 38.21 A C ANISOU 362 CD1 LEU A 53 4861 5213 4442 -120 -88 914 A C ATOM 363 CD2 LEU A 53 -49.189 19.882 51.547 1.00 38.66 A C ANISOU 363 CD2 LEU A 53 5058 5003 4629 -282 -16 840 A C ATOM 364 N PRO A 54 -49.461 14.592 49.198 1.00 31.77 A N ANISOU 364 N PRO A 54 3938 4140 3995 -372 212 1444 A N ATOM 365 CA PRO A 54 -49.232 14.274 47.787 1.00 32.94 A C ANISOU 365 CA PRO A 54 4243 4060 4214 -374 314 1479 A C ATOM 366 C PRO A 54 -50.298 14.850 46.867 1.00 37.24 A C ANISOU 366 C PRO A 54 5014 4501 4633 -248 286 1398 A C ATOM 367 O PRO A 54 -51.389 15.241 47.287 1.00 41.92 A O ANISOU 367 O PRO A 54 5602 5222 5102 -136 176 1313 A O ATOM 368 CB PRO A 54 -49.303 12.743 47.772 1.00 32.79 A C ANISOU 368 CB PRO A 54 4059 4115 4285 -402 321 1608 A C ATOM 369 CG PRO A 54 -50.306 12.435 48.837 1.00 25.92 A C ANISOU 369 CG PRO A 54 3046 3501 3303 -371 206 1624 A C ATOM 370 CD PRO A 54 -50.112 13.478 49.912 1.00 33.34 A C ANISOU 370 CD PRO A 54 3940 4564 4163 -379 147 1537 A C ATOM 371 N MET A 55 -49.957 14.882 45.582 1.00 36.67 A N ANISOU 371 N MET A 55 5136 4208 4590 -268 381 1413 A N ATOM 372 CA MET A 55 -50.914 15.178 44.528 1.00 38.29 A C ANISOU 372 CA MET A 55 5567 4302 4681 -147 347 1366 A C ATOM 373 C MET A 55 -50.772 14.154 43.411 1.00 38.70 A C ANISOU 373 C MET A 55 5642 4268 4794 -183 448 1437 A C ATOM 374 O MET A 55 -49.672 13.677 43.116 1.00 37.57 A O ANISOU 374 O MET A 55 5446 4053 4777 -312 573 1490 A O ATOM 375 CB MET A 55 -50.729 16.594 43.964 1.00 38.81 A C ANISOU 375 CB MET A 55 5944 4142 4659 -129 339 1293 A C ATOM 376 CG MET A 55 -49.561 16.744 43.008 1.00 37.92 A C ANISOU 376 CG MET A 55 5999 3811 4597 -291 503 1342 A C ATOM 377 SD MET A 55 -49.466 18.409 42.325 1.00 43.32 A S ANISOU 377 SD MET A 55 7110 4203 5145 -300 479 1285 A S ATOM 378 CE MET A 55 -48.370 18.139 40.935 1.00 42.75 A C ANISOU 378 CE MET A 55 7149 3989 5107 -502 679 1324 A C ATOM 379 N ALA A 56 -51.900 13.819 42.791 1.00 39.81 A N ANISOU 379 N ALA A 56 5844 4431 4849 -62 387 1411 A N ATOM 380 CA ALA A 56 -51.876 12.922 41.645 1.00 38.01 A C ANISOU 380 CA ALA A 56 5659 4120 4662 -83 473 1452 A C ATOM 381 C ALA A 56 -51.310 13.640 40.427 1.00 41.42 A C ANISOU 381 C ALA A 56 6389 4318 5031 -129 564 1438 A C ATOM 382 O ALA A 56 -51.569 14.827 40.208 1.00 42.65 A O ANISOU 382 O ALA A 56 6791 4358 5054 -70 499 1391 A O ATOM 383 CB ALA A 56 -53.278 12.395 41.346 1.00 36.16 A C ANISOU 383 CB ALA A 56 5399 3995 4346 53 376 1407 A C ATOM 384 N LEU A 57 -50.528 12.916 39.639 1.00 42.01 A N ANISOU 384 N LEU A 57 6418 4346 5199 -245 684 1444 A N ATOM 385 CA LEU A 57 -49.881 13.475 38.464 1.00 45.42 A C ANISOU 385 CA LEU A 57 7031 4653 5575 -333 752 1381 A C ATOM 386 C LEU A 57 -50.682 13.181 37.199 1.00 48.74 A C ANISOU 386 C LEU A 57 7602 5032 5886 -250 735 1351 A C ATOM 387 O LEU A 57 -51.581 12.336 37.175 1.00 50.87 A O ANISOU 387 O LEU A 57 7801 5369 6157 -146 693 1371 A O ATOM 388 CB LEU A 57 -48.457 12.926 38.334 1.00 44.51 A C ANISOU 388 CB LEU A 57 6747 4555 5609 -505 888 1357 A C ATOM 389 CG LEU A 57 -47.472 13.355 39.421 1.00 43.72 A C ANISOU 389 CG LEU A 57 6526 4480 5605 -606 918 1364 A C ATOM 390 CD1 LEU A 57 -46.111 12.702 39.222 1.00 44.93 A C ANISOU 390 CD1 LEU A 57 6504 4661 5908 -747 1047 1314 A C ATOM 391 CD2 LEU A 57 -47.345 14.872 39.449 1.00 46.38 A C ANISOU 391 CD2 LEU A 57 7088 4707 5827 -637 905 1343 A C ATOM 392 N GLU A 58 -50.345 13.914 36.136 1.00 51.88 A N ANISOU 392 N GLU A 58 8219 5319 6173 -305 774 1306 A N ATOM 393 CA GLU A 58 -50.879 13.617 34.814 1.00 53.68 A C ANISOU 393 CA GLU A 58 8603 5507 6285 -260 782 1278 A C ATOM 394 C GLU A 58 -50.185 12.421 34.178 1.00 52.58 A C ANISOU 394 C GLU A 58 8312 5413 6253 -370 936 1260 A C ATOM 395 O GLU A 58 -50.710 11.857 33.212 1.00 56.16 A O ANISOU 395 O GLU A 58 8848 5856 6634 -326 958 1241 A O ATOM 396 CB GLU A 58 -50.765 14.841 33.901 1.00 59.68 A C ANISOU 396 CB GLU A 58 9675 6132 6867 -291 765 1246 A C ATOM 397 CG GLU A 58 -51.832 15.899 34.150 1.00 67.73 A C ANISOU 397 CG GLU A 58 10913 7073 7749 -115 569 1237 A C ATOM 398 CD GLU A 58 -51.446 17.268 33.610 1.00 75.33 A C ANISOU 398 CD GLU A 58 12166 7875 8582 -182 546 1219 A C ATOM 399 OE1 GLU A 58 -50.324 17.733 33.910 1.00 75.35 A O ANISOU 399 OE1 GLU A 58 12138 7844 8648 -354 653 1226 A O ATOM 400 OE2 GLU A 58 -52.264 17.872 32.880 1.00 78.39 A O1- ANISOU 400 OE2 GLU A 58 12818 8166 8802 -62 413 1195 A O1- ATOM 401 N LEU A 59 -49.031 12.018 34.706 1.00 48.37 A N ANISOU 401 N LEU A 59 7566 4924 5888 -501 1039 1254 A N ATOM 402 CA LEU A 59 -48.416 10.760 34.306 1.00 46.20 A C ANISOU 402 CA LEU A 59 7111 4688 5756 -573 1168 1221 A C ATOM 403 C LEU A 59 -49.289 9.603 34.773 1.00 46.70 A C ANISOU 403 C LEU A 59 7009 4811 5924 -454 1099 1264 A C ATOM 404 O LEU A 59 -49.829 9.620 35.883 1.00 51.48 A O ANISOU 404 O LEU A 59 7518 5476 6567 -378 984 1322 A O ATOM 405 CB LEU A 59 -47.008 10.653 34.886 1.00 44.38 A C ANISOU 405 CB LEU A 59 6686 4487 5688 -710 1266 1188 A C ATOM 406 CG LEU A 59 -46.118 11.852 34.553 1.00 43.20 A C ANISOU 406 CG LEU A 59 6684 4290 5442 -848 1342 1145 A C ATOM 407 CD1 LEU A 59 -44.721 11.665 35.119 1.00 43.30 A C ANISOU 407 CD1 LEU A 59 6480 4348 5623 -983 1451 1090 A C ATOM 408 CD2 LEU A 59 -46.061 12.076 33.049 1.00 32.94 A C ANISOU 408 CD2 LEU A 59 5604 2933 3978 -920 1446 1089 A C ATOM 409 N MET A 60 -49.426 8.589 33.922 1.00 47.09 A N ANISOU 409 N MET A 60 7027 4846 6020 -451 1184 1232 A N ATOM 410 CA MET A 60 -50.569 7.699 34.042 1.00 44.78 A C ANISOU 410 CA MET A 60 6667 4584 5764 -328 1113 1274 A C ATOM 411 C MET A 60 -50.236 6.285 33.588 1.00 41.68 A C ANISOU 411 C MET A 60 6099 4169 5567 -363 1223 1242 A C ATOM 412 O MET A 60 -49.340 6.068 32.768 1.00 39.68 A O ANISOU 412 O MET A 60 5852 3867 5356 -464 1379 1162 A O ATOM 413 CB MET A 60 -51.722 8.262 33.204 1.00 46.20 A C ANISOU 413 CB MET A 60 7124 4729 5700 -219 1053 1268 A C ATOM 414 CG MET A 60 -53.106 7.775 33.533 1.00 48.11 A C ANISOU 414 CG MET A 60 7292 5065 5922 -66 907 1269 A C ATOM 415 SD MET A 60 -54.237 8.618 32.415 1.00 50.31 A S ANISOU 415 SD MET A 60 7903 5313 5899 78 798 1207 A S ATOM 416 CE MET A 60 -53.326 10.138 32.142 1.00 49.08 A C ANISOU 416 CE MET A 60 8036 5015 5598 -14 840 1240 A C ATOM 417 N THR A 61 -50.965 5.327 34.154 1.00 39.65 A N ANISOU 417 N THR A 61 5663 3969 5431 -288 1120 1276 A N ATOM 418 CA THR A 61 -51.046 3.965 33.645 1.00 42.89 A C ANISOU 418 CA THR A 61 5926 4368 6003 -284 1143 1211 A C ATOM 419 C THR A 61 -52.454 3.733 33.116 1.00 45.02 A C ANISOU 419 C THR A 61 6275 4695 6137 -186 1055 1172 A C ATOM 420 O THR A 61 -53.436 3.980 33.825 1.00 43.96 A O ANISOU 420 O THR A 61 6131 4647 5923 -116 925 1223 A O ATOM 421 CB THR A 61 -50.716 2.937 34.728 1.00 41.64 A C ANISOU 421 CB THR A 61 5503 4210 6109 -299 1076 1280 A C ATOM 422 CG2 THR A 61 -50.918 1.519 34.198 1.00 43.67 A C ANISOU 422 CG2 THR A 61 5632 4419 6539 -287 1075 1210 A C ATOM 423 OG1 THR A 61 -49.356 3.101 35.146 1.00 42.10 A O ANISOU 423 OG1 THR A 61 5466 4226 6306 -372 1146 1284 A O ATOM 424 N VAL A 62 -52.552 3.255 31.880 1.00 44.61 A N ANISOU 424 N VAL A 62 6282 4614 6053 -186 1127 1059 A N ATOM 425 CA VAL A 62 -53.826 2.904 31.264 1.00 41.72 A C ANISOU 425 CA VAL A 62 5967 4310 5577 -95 1047 990 A C ATOM 426 C VAL A 62 -53.842 1.401 31.028 1.00 41.57 A C ANISOU 426 C VAL A 62 5745 4267 5783 -122 1067 918 A C ATOM 427 O VAL A 62 -52.879 0.837 30.494 1.00 44.43 A O ANISOU 427 O VAL A 62 6040 4553 6289 -186 1184 844 A O ATOM 428 CB VAL A 62 -54.058 3.678 29.957 1.00 42.21 A C ANISOU 428 CB VAL A 62 6305 4362 5371 -62 1086 912 A C ATOM 429 CG1 VAL A 62 -55.291 3.150 29.254 1.00 41.28 A C ANISOU 429 CG1 VAL A 62 6201 4318 5165 36 1000 809 A C ATOM 430 CG2 VAL A 62 -54.211 5.161 30.250 1.00 40.32 A C ANISOU 430 CG2 VAL A 62 6295 4110 4914 -18 1021 991 A C ATOM 431 N LEU A 63 -54.932 0.756 31.432 1.00 40.48 A N ANISOU 431 N LEU A 63 5503 4196 5681 -80 953 922 A N ATOM 432 CA LEU A 63 -55.115 -0.678 31.264 1.00 39.55 A C ANISOU 432 CA LEU A 63 5215 4037 5776 -113 948 860 A C ATOM 433 C LEU A 63 -56.344 -0.938 30.405 1.00 38.10 A C ANISOU 433 C LEU A 63 5082 3939 5458 -51 902 730 A C ATOM 434 O LEU A 63 -57.437 -0.448 30.713 1.00 36.49 A O ANISOU 434 O LEU A 63 4915 3861 5090 11 799 736 A O ATOM 435 CB LEU A 63 -55.259 -1.359 32.626 1.00 40.64 A C ANISOU 435 CB LEU A 63 5174 4169 6097 -166 854 993 A C ATOM 436 CG LEU A 63 -55.066 -2.873 32.680 1.00 44.77 A C ANISOU 436 CG LEU A 63 5535 4572 6903 -226 840 976 A C ATOM 437 CD1 LEU A 63 -53.696 -3.254 32.142 1.00 47.55 A C ANISOU 437 CD1 LEU A 63 5843 4778 7446 -234 937 903 A C ATOM 438 CD2 LEU A 63 -55.247 -3.375 34.105 1.00 46.75 A C ANISOU 438 CD2 LEU A 63 5669 4817 7276 -298 731 1150 A C ATOM 439 N VAL A 64 -56.160 -1.696 29.325 1.00 36.75 A N ANISOU 439 N VAL A 64 4895 3713 5355 -63 975 586 A N ATOM 440 CA VAL A 64 -57.259 -2.153 28.484 1.00 38.34 A C ANISOU 440 CA VAL A 64 5109 3993 5466 -15 931 438 A C ATOM 441 C VAL A 64 -57.255 -3.675 28.456 1.00 37.79 A C ANISOU 441 C VAL A 64 4847 3835 5678 -83 937 366 A C ATOM 442 O VAL A 64 -56.199 -4.314 28.509 1.00 41.35 A O ANISOU 442 O VAL A 64 5206 4144 6361 -135 1004 366 A O ATOM 443 CB VAL A 64 -57.166 -1.586 27.050 1.00 38.39 A C ANISOU 443 CB VAL A 64 5314 4028 5243 36 1002 307 A C ATOM 444 CG1 VAL A 64 -57.052 -0.070 27.082 1.00 35.82 A C ANISOU 444 CG1 VAL A 64 5222 3736 4653 88 986 400 A C ATOM 445 CG2 VAL A 64 -55.992 -2.203 26.314 1.00 32.23 A C ANISOU 445 CG2 VAL A 64 4489 3147 4612 -41 1155 210 A C ATOM 446 N GLY A 65 -58.446 -4.255 28.374 1.00 35.95 A N ANISOU 446 N GLY A 65 4548 3681 5432 -80 857 288 A N ATOM 447 CA GLY A 65 -58.555 -5.702 28.345 1.00 39.44 A C ANISOU 447 CA GLY A 65 4829 4018 6137 -159 849 218 A C ATOM 448 C GLY A 65 -59.996 -6.143 28.200 1.00 37.72 A C ANISOU 448 C GLY A 65 4554 3929 5849 -170 769 113 A C ATOM 449 O GLY A 65 -60.912 -5.330 28.028 1.00 37.57 A O ANISOU 449 O GLY A 65 4606 4095 5575 -91 713 64 A O ATOM 450 N SER A 66 -60.180 -7.459 28.275 1.00 40.96 A N ANISOU 450 N SER A 66 4832 4230 6502 -270 753 62 A N ATOM 451 CA SER A 66 -61.473 -8.107 28.109 1.00 41.25 A C ANISOU 451 CA SER A 66 4783 4368 6523 -325 695 -65 A C ATOM 452 C SER A 66 -61.485 -9.383 28.934 1.00 40.86 A C ANISOU 452 C SER A 66 4609 4152 6764 -494 657 24 A C ATOM 453 O SER A 66 -60.421 -9.957 29.195 1.00 39.82 A O ANISOU 453 O SER A 66 4464 3791 6877 -524 672 113 A O ATOM 454 CB SER A 66 -61.763 -8.429 26.636 1.00 41.80 A C ANISOU 454 CB SER A 66 4873 4472 6535 -259 731 -326 A C ATOM 455 OG SER A 66 -61.670 -7.266 25.831 1.00 46.62 A O ANISOU 455 OG SER A 66 5642 5210 6860 -115 755 -384 A O ATOM 456 N PRO A 67 -62.654 -9.842 29.368 1.00 42.15 A N ANISOU 456 N PRO A 67 4687 4423 6907 -613 602 -0 A N ATOM 457 CA PRO A 67 -62.730 -11.137 30.051 1.00 42.57 A C ANISOU 457 CA PRO A 67 4658 4292 7225 -809 564 85 A C ATOM 458 C PRO A 67 -62.452 -12.284 29.092 1.00 45.49 A C ANISOU 458 C PRO A 67 4998 4452 7835 -821 583 -92 A C ATOM 459 O PRO A 67 -62.597 -12.166 27.873 1.00 49.62 A O ANISOU 459 O PRO A 67 5528 5048 8276 -711 628 -324 A O ATOM 460 CB PRO A 67 -64.171 -11.186 30.569 1.00 43.24 A C ANISOU 460 CB PRO A 67 4656 4607 7166 -948 527 49 A C ATOM 461 CG PRO A 67 -64.925 -10.282 29.651 1.00 45.24 A C ANISOU 461 CG PRO A 67 4915 5129 7146 -784 534 -172 A C ATOM 462 CD PRO A 67 -63.970 -9.191 29.254 1.00 44.78 A C ANISOU 462 CD PRO A 67 4991 5052 6970 -580 564 -121 A C ATOM 463 N ARG A 68 -62.026 -13.406 29.665 1.00 47.55 A N ANISOU 463 N ARG A 68 5235 4438 8393 -953 535 18 A N ATOM 464 CA ARG A 68 -61.761 -14.622 28.913 1.00 48.60 A C ANISOU 464 CA ARG A 68 5333 4327 8804 -975 528 -148 A C ATOM 465 C ARG A 68 -62.615 -15.765 29.447 1.00 56.28 A C ANISOU 465 C ARG A 68 6266 5187 9929 -1213 460 -114 A C ATOM 466 O ARG A 68 -63.089 -15.739 30.585 1.00 58.98 A O ANISOU 466 O ARG A 68 6620 5581 10210 -1379 417 96 A O ATOM 467 CB ARG A 68 -60.277 -15.014 28.978 1.00 48.71 A C ANISOU 467 CB ARG A 68 5369 4046 9094 -887 509 -82 A C ATOM 468 CG ARG A 68 -59.314 -14.005 28.374 1.00 45.31 A C ANISOU 468 CG ARG A 68 4967 3709 8541 -692 598 -143 A C ATOM 469 CD ARG A 68 -57.872 -14.373 28.700 1.00 45.31 A C ANISOU 469 CD ARG A 68 4952 3447 8817 -626 568 -69 A C ATOM 470 NE ARG A 68 -57.482 -15.645 28.098 1.00 48.49 A N ANISOU 470 NE ARG A 68 5289 3584 9550 -616 531 -256 A N ATOM 471 CZ ARG A 68 -56.696 -15.763 27.032 1.00 48.65 A C ANISOU 471 CZ ARG A 68 5253 3568 9662 -490 610 -509 A C ATOM 472 NH1 ARG A 68 -56.199 -14.682 26.445 1.00 47.16 A N1+ ANISOU 472 NH1 ARG A 68 5086 3590 9244 -388 739 -582 A N1+ ATOM 473 NH2 ARG A 68 -56.400 -16.967 26.558 1.00 50.74 A N ANISOU 473 NH2 ARG A 68 5446 3586 10246 -478 560 -698 A N ATOM 474 N LYS A 69 -62.807 -16.774 28.601 1.00 60.45 A N ANISOU 474 N LYS A 69 6752 5568 10648 -1246 457 -335 A N ATOM 475 CA LYS A 69 -63.423 -18.030 28.999 1.00 63.42 A C ANISOU 475 CA LYS A 69 7113 5750 11232 -1486 390 -316 A C ATOM 476 C LYS A 69 -62.397 -19.043 29.485 1.00 64.72 A C ANISOU 476 C LYS A 69 7346 5477 11768 -1518 287 -167 A C ATOM 477 O LYS A 69 -62.780 -20.095 30.000 1.00 66.17 A O ANISOU 477 O LYS A 69 7568 5434 12139 -1735 206 -81 A O ATOM 478 CB LYS A 69 -64.225 -18.617 27.829 1.00 62.60 A C ANISOU 478 CB LYS A 69 6927 5705 11152 -1512 427 -655 A C ATOM 479 CG LYS A 69 -65.174 -17.625 27.163 1.00 62.40 A C ANISOU 479 CG LYS A 69 6836 6103 10768 -1425 499 -847 A C ATOM 480 CD LYS A 69 -66.245 -17.135 28.127 1.00 65.69 A C ANISOU 480 CD LYS A 69 7216 6786 10958 -1587 491 -720 A C ATOM 481 CE LYS A 69 -67.078 -16.017 27.510 1.00 67.02 A C ANISOU 481 CE LYS A 69 7323 7365 10776 -1439 526 -911 A C ATOM 482 NZ LYS A 69 -67.924 -16.487 26.375 1.00 69.44 A N1+ ANISOU 482 NZ LYS A 69 7535 7787 11062 -1440 536 -1255 A N1+ ATOM 483 N ASP A 70 -61.107 -18.740 29.329 1.00 70.10 A N ANISOU 483 N ASP A 70 8046 6033 12555 -1309 281 -142 A N ATOM 484 CA ASP A 70 -60.038 -19.694 29.583 1.00 75.17 A C ANISOU 484 CA ASP A 70 8725 6261 13575 -1270 164 -78 A C ATOM 485 C ASP A 70 -59.797 -19.941 31.063 1.00 71.21 A C ANISOU 485 C ASP A 70 8344 5670 13042 -1365 30 285 A C ATOM 486 O ASP A 70 -59.248 -20.989 31.422 1.00 70.34 A O ANISOU 486 O ASP A 70 8316 5322 13088 -1343 -110 352 A O ATOM 487 CB ASP A 70 -58.731 -19.174 28.976 1.00 82.84 A C ANISOU 487 CB ASP A 70 9651 7222 14604 -1006 212 -198 A C ATOM 488 CG ASP A 70 -58.536 -19.588 27.537 1.00 90.22 A C ANISOU 488 CG ASP A 70 10498 8131 15649 -885 284 -576 A C ATOM 489 OD1 ASP A 70 -59.469 -20.174 26.957 1.00 93.78 A O ANISOU 489 OD1 ASP A 70 10924 8602 16108 -988 299 -753 A O ATOM 490 OD2 ASP A 70 -57.440 -19.312 26.992 1.00 91.45 A O1- ANISOU 490 OD2 ASP A 70 10601 8271 15876 -699 334 -710 A O1- ATOM 491 N GLY A 71 -60.200 -19.013 31.925 1.00 69.43 A N ANISOU 491 N GLY A 71 8141 5676 12563 -1453 64 500 A N ATOM 492 CA GLY A 71 -59.691 -19.054 33.277 1.00 66.17 A C ANISOU 492 CA GLY A 71 7848 5249 12045 -1471 -51 805 A C ATOM 493 C GLY A 71 -58.237 -18.654 33.365 1.00 63.90 A C ANISOU 493 C GLY A 71 7548 4886 11844 -1226 -93 842 A C ATOM 494 O GLY A 71 -57.608 -18.848 34.411 1.00 61.85 A O ANISOU 494 O GLY A 71 7375 4572 11554 -1205 -214 1051 A O ATOM 495 N LEU A 72 -57.684 -18.111 32.285 1.00 61.89 A N ANISOU 495 N LEU A 72 7186 4636 11695 -1053 11 621 A N ATOM 496 CA LEU A 72 -56.297 -17.685 32.204 1.00 60.44 A C ANISOU 496 CA LEU A 72 6957 4403 11604 -838 5 597 A C ATOM 497 C LEU A 72 -56.194 -16.166 32.258 1.00 60.49 A C ANISOU 497 C LEU A 72 6938 4647 11396 -793 137 655 A C ATOM 498 O LEU A 72 -57.144 -15.441 31.947 1.00 43.53 A O ANISOU 498 O LEU A 72 4793 2766 8979 -849 247 608 A O ATOM 499 CB LEU A 72 -55.642 -18.194 30.916 1.00 48.97 A C ANISOU 499 CB LEU A 72 5405 2786 10417 -688 48 272 A C ATOM 500 CG LEU A 72 -55.704 -19.697 30.647 1.00 55.85 A C ANISOU 500 CG LEU A 72 6285 3410 11525 -705 -76 157 A C ATOM 501 CD1 LEU A 72 -55.008 -20.037 29.337 1.00 53.02 A C ANISOU 501 CD1 LEU A 72 5798 2954 11394 -539 -13 -207 A C ATOM 502 CD2 LEU A 72 -55.073 -20.449 31.802 1.00 53.99 A C ANISOU 502 CD2 LEU A 72 6137 3009 11367 -690 -285 388 A C ATOM 503 N VAL A 73 -55.012 -15.694 32.645 1.00 44.45 A N ANISOU 503 N VAL A 73 4888 2616 9385 -655 113 722 A N ATOM 504 CA VAL A 73 -54.666 -14.278 32.613 1.00 58.31 A C ANISOU 504 CA VAL A 73 6630 4587 10939 -585 239 748 A C ATOM 505 C VAL A 73 -53.550 -14.095 31.595 1.00 54.70 A C ANISOU 505 C VAL A 73 6086 4106 10589 -413 334 493 A C ATOM 506 O VAL A 73 -52.493 -14.730 31.699 1.00 55.34 A O ANISOU 506 O VAL A 73 6098 3958 10971 -323 249 446 A O ATOM 507 CB VAL A 73 -54.240 -13.761 33.996 1.00 41.38 A C ANISOU 507 CB VAL A 73 4529 2533 8661 -595 146 1020 A C ATOM 508 CG1 VAL A 73 -53.859 -12.284 33.922 1.00 40.90 A C ANISOU 508 CG1 VAL A 73 4459 2669 8413 -529 278 1035 A C ATOM 509 CG2 VAL A 73 -55.354 -13.974 34.999 1.00 42.95 A C ANISOU 509 CG2 VAL A 73 4814 2845 8660 -771 67 1221 A C ATOM 510 N SER A 74 -53.785 -13.227 30.615 1.00 53.90 A N ANISOU 510 N SER A 74 5993 4249 10238 -370 504 321 A N ATOM 511 CA SER A 74 -52.811 -12.927 29.573 1.00 55.77 A C ANISOU 511 CA SER A 74 6163 4524 10502 -252 634 71 A C ATOM 512 C SER A 74 -52.485 -11.442 29.634 1.00 51.65 A C ANISOU 512 C SER A 74 5700 4242 9680 -229 753 141 A C ATOM 513 O SER A 74 -53.379 -10.601 29.493 1.00 47.48 A O ANISOU 513 O SER A 74 5277 3924 8840 -266 809 193 A O ATOM 514 CB SER A 74 -53.350 -13.310 28.193 1.00 61.69 A C ANISOU 514 CB SER A 74 6898 5329 11211 -244 731 -217 A C ATOM 515 OG SER A 74 -52.304 -13.738 27.339 1.00 66.75 A O ANISOU 515 OG SER A 74 7427 5885 12051 -151 797 -487 A O ATOM 516 N LEU A 75 -51.209 -11.123 29.844 1.00 51.82 A N ANISOU 516 N LEU A 75 5654 4230 9807 -166 781 127 A N ATOM 517 CA LEU A 75 -50.767 -9.758 30.082 1.00 45.39 A C ANISOU 517 CA LEU A 75 4896 3600 8749 -166 878 216 A C ATOM 518 C LEU A 75 -49.718 -9.341 29.063 1.00 43.70 A C ANISOU 518 C LEU A 75 4627 3461 8517 -126 1052 -30 A C ATOM 519 O LEU A 75 -48.924 -10.159 28.589 1.00 46.09 A O ANISOU 519 O LEU A 75 4784 3644 9084 -72 1061 -243 A O ATOM 520 CB LEU A 75 -50.166 -9.593 31.485 1.00 43.98 A C ANISOU 520 CB LEU A 75 4684 3351 8676 -164 755 451 A C ATOM 521 CG LEU A 75 -50.947 -10.050 32.713 1.00 43.79 A C ANISOU 521 CG LEU A 75 4704 3247 8686 -231 576 720 A C ATOM 522 CD1 LEU A 75 -50.087 -9.873 33.946 1.00 42.66 A C ANISOU 522 CD1 LEU A 75 4519 3043 8648 -212 464 910 A C ATOM 523 CD2 LEU A 75 -52.240 -9.258 32.842 1.00 45.17 A C ANISOU 523 CD2 LEU A 75 5003 3636 8523 -308 615 828 A C ATOM 524 N LEU A 76 -49.735 -8.053 28.725 1.00 43.79 A N ANISOU 524 N LEU A 76 4759 3672 8206 -163 1188 -9 A N ATOM 525 CA LEU A 76 -48.677 -7.439 27.936 1.00 45.14 A C ANISOU 525 CA LEU A 76 4906 3940 8304 -178 1371 -193 A C ATOM 526 C LEU A 76 -48.487 -6.006 28.405 1.00 44.84 A C ANISOU 526 C LEU A 76 5000 4035 8002 -230 1432 -25 A C ATOM 527 O LEU A 76 -49.456 -5.245 28.486 1.00 44.20 A O ANISOU 527 O LEU A 76 5099 4049 7646 -248 1413 116 A O ATOM 528 CB LEU A 76 -49.002 -7.465 26.439 1.00 45.90 A C ANISOU 528 CB LEU A 76 5067 4143 8231 -201 1517 -431 A C ATOM 529 CG LEU A 76 -48.094 -6.603 25.559 1.00 43.82 A C ANISOU 529 CG LEU A 76 4843 4030 7777 -272 1736 -591 A C ATOM 530 CD1 LEU A 76 -47.777 -7.312 24.251 1.00 47.49 A C ANISOU 530 CD1 LEU A 76 5214 4531 8299 -279 1861 -924 A C ATOM 531 CD2 LEU A 76 -48.720 -5.241 25.300 1.00 42.88 A C ANISOU 531 CD2 LEU A 76 4996 4063 7235 -334 1801 -447 A C ATOM 532 N THR A 77 -47.248 -5.646 28.720 1.00 46.35 A N ANISOU 532 N THR A 77 5091 4231 8289 -247 1494 -61 A N ATOM 533 CA THR A 77 -46.881 -4.271 29.018 1.00 45.01 A C ANISOU 533 CA THR A 77 5039 4179 7883 -319 1582 49 A C ATOM 534 C THR A 77 -45.921 -3.771 27.948 1.00 48.19 A C ANISOU 534 C THR A 77 5439 4687 8182 -410 1811 -180 A C ATOM 535 O THR A 77 -45.025 -4.503 27.514 1.00 48.22 A O ANISOU 535 O THR A 77 5239 4669 8413 -400 1877 -416 A O ATOM 536 CB THR A 77 -46.239 -4.146 30.404 1.00 46.39 A C ANISOU 536 CB THR A 77 5102 4298 8225 -297 1466 208 A C ATOM 537 CG2 THR A 77 -44.999 -5.021 30.499 1.00 49.43 A C ANISOU 537 CG2 THR A 77 5228 4591 8963 -246 1450 29 A C ATOM 538 OG1 THR A 77 -45.868 -2.782 30.643 1.00 42.05 A O ANISOU 538 OG1 THR A 77 4668 3860 7450 -377 1560 289 A O ATOM 539 N THR A 78 -46.117 -2.528 27.520 1.00 47.71 A N ANISOU 539 N THR A 78 5610 4742 7776 -505 1928 -118 A N ATOM 540 CA THR A 78 -45.268 -1.905 26.516 1.00 47.01 A C ANISOU 540 CA THR A 78 5573 4766 7521 -645 2162 -299 A C ATOM 541 C THR A 78 -44.177 -1.040 27.132 1.00 48.54 A C ANISOU 541 C THR A 78 5726 4999 7719 -745 2244 -265 A C ATOM 542 O THR A 78 -43.463 -0.345 26.401 1.00 52.42 A O ANISOU 542 O THR A 78 6287 5593 8036 -907 2453 -388 A O ATOM 543 CB THR A 78 -46.113 -1.076 25.549 1.00 47.92 A C ANISOU 543 CB THR A 78 6010 4964 7233 -709 2236 -255 A C ATOM 544 CG2 THR A 78 -47.245 -1.921 24.982 1.00 38.08 A C ANISOU 544 CG2 THR A 78 4788 3698 5981 -605 2141 -302 A C ATOM 545 OG1 THR A 78 -46.664 0.051 26.241 1.00 46.41 A O ANISOU 545 OG1 THR A 78 6038 4762 6834 -708 2150 -2 A O ATOM 546 N SER A 79 -44.030 -1.072 28.452 1.00 51.33 A N ANISOU 546 N SER A 79 5968 5281 8256 -671 2089 -107 A N ATOM 547 CA SER A 79 -43.053 -0.231 29.129 1.00 57.88 A C ANISOU 547 CA SER A 79 6749 6152 9090 -759 2146 -74 A C ATOM 548 C SER A 79 -41.654 -0.801 28.944 1.00 68.25 A C ANISOU 548 C SER A 79 7761 7504 10667 -791 2251 -347 A C ATOM 549 O SER A 79 -41.416 -1.986 29.196 1.00 66.61 A O ANISOU 549 O SER A 79 7313 7216 10781 -657 2133 -449 A O ATOM 550 CB SER A 79 -43.387 -0.122 30.615 1.00 55.22 A C ANISOU 550 CB SER A 79 6384 5747 8851 -662 1932 172 A C ATOM 551 OG SER A 79 -44.709 0.349 30.800 1.00 54.08 A O ANISOU 551 OG SER A 79 6478 5591 8479 -622 1832 381 A O ATOM 552 N GLU A 80 -40.724 0.055 28.520 1.00 82.63 A N ANISOU 552 N GLU A 80 9594 9446 12355 -974 2466 -475 A N ATOM 553 CA GLU A 80 -39.390 -0.421 28.172 1.00 88.66 A C ANISOU 553 CA GLU A 80 10053 10298 13338 -1028 2603 -798 A C ATOM 554 C GLU A 80 -38.573 -0.797 29.402 1.00 86.75 A C ANISOU 554 C GLU A 80 9520 10010 13430 -914 2446 -808 A C ATOM 555 O GLU A 80 -37.757 -1.722 29.337 1.00 88.95 A O ANISOU 555 O GLU A 80 9487 10293 14017 -828 2425 -1064 A O ATOM 556 CB GLU A 80 -38.654 0.641 27.362 1.00 93.79 A C ANISOU 556 CB GLU A 80 10806 11111 13718 -1301 2897 -936 A C ATOM 557 N GLY A 81 -38.761 -0.087 30.513 1.00 79.73 A N ANISOU 557 N GLY A 81 8725 9084 12485 -904 2325 -553 A N ATOM 558 CA GLY A 81 -38.023 -0.349 31.735 1.00 74.48 A C ANISOU 558 CA GLY A 81 7814 8390 12096 -801 2160 -537 A C ATOM 559 C GLY A 81 -38.511 -1.585 32.459 1.00 72.73 A C ANISOU 559 C GLY A 81 7482 8003 12148 -567 1874 -426 A C ATOM 560 O GLY A 81 -38.034 -1.916 33.550 1.00 71.22 A O ANISOU 560 O GLY A 81 7121 7760 12180 -455 1683 -369 A O ATOM 561 N ALA A 82 -39.444 -2.293 31.837 1.00 68.27 A N ANISOU 561 N ALA A 82 7023 7353 11565 -502 1838 -401 A N ATOM 562 CA ALA A 82 -40.075 -3.429 32.473 1.00 64.06 A C ANISOU 562 CA ALA A 82 6446 6643 11252 -321 1577 -265 A C ATOM 563 C ALA A 82 -39.188 -4.667 32.410 1.00 63.68 A C ANISOU 563 C ALA A 82 6095 6501 11599 -180 1478 -514 A C ATOM 564 O ALA A 82 -38.328 -4.815 31.536 1.00 65.96 A O ANISOU 564 O ALA A 82 6209 6878 11975 -213 1643 -845 A O ATOM 565 CB ALA A 82 -41.425 -3.698 31.819 1.00 59.92 A C ANISOU 565 CB ALA A 82 6139 6069 10559 -320 1579 -166 A C ATOM 566 N ASP A 83 -39.426 -5.565 33.362 1.00 63.56 A N ANISOU 566 N ASP A 83 6027 6304 11819 -23 1196 -355 A N ATOM 567 CA ASP A 83 -38.681 -6.812 33.452 1.00 66.35 A C ANISOU 567 CA ASP A 83 6126 6508 12575 152 1028 -553 A C ATOM 568 C ASP A 83 -39.010 -7.707 32.262 1.00 68.19 A C ANISOU 568 C ASP A 83 6335 6668 12905 188 1096 -779 A C ATOM 569 O ASP A 83 -40.182 -7.929 31.944 1.00 69.59 A O ANISOU 569 O ASP A 83 6714 6782 12946 158 1090 -633 A O ATOM 570 CB ASP A 83 -39.017 -7.527 34.765 1.00 68.53 A C ANISOU 570 CB ASP A 83 6432 6576 13029 286 692 -268 A C ATOM 571 CG ASP A 83 -37.937 -8.510 35.200 1.00 74.87 A C ANISOU 571 CG ASP A 83 6971 7232 14246 483 468 -441 A C ATOM 572 OD1 ASP A 83 -36.817 -8.060 35.514 1.00 78.94 A O ANISOU 572 OD1 ASP A 83 7287 7866 14841 506 486 -592 A O ATOM 573 OD2 ASP A 83 -38.211 -9.729 35.245 1.00 77.64 A O1- ANISOU 573 OD2 ASP A 83 7315 7339 14847 618 259 -431 A O1- ATOM 574 N GLU A 84 -37.976 -8.218 31.599 1.00 68.43 A N ANISOU 574 N GLU A 84 6100 6728 13174 254 1162 -1163 A N ATOM 575 CA GLU A 84 -38.260 -9.123 30.493 1.00 69.73 A C ANISOU 575 CA GLU A 84 6221 6824 13448 299 1215 -1406 A C ATOM 576 C GLU A 84 -38.559 -10.523 31.029 1.00 66.87 A C ANISOU 576 C GLU A 84 5820 6146 13441 503 892 -1339 A C ATOM 577 O GLU A 84 -37.920 -10.972 31.984 1.00 65.40 A O ANISOU 577 O GLU A 84 5503 5820 13527 652 649 -1296 A O ATOM 578 CB GLU A 84 -37.084 -9.177 29.519 1.00 76.83 A C ANISOU 578 CB GLU A 84 6839 7892 14460 284 1420 -1883 A C ATOM 579 CG GLU A 84 -37.421 -9.813 28.175 1.00 83.99 A C ANISOU 579 CG GLU A 84 7728 8815 15368 270 1559 -2162 A C ATOM 580 CD GLU A 84 -37.057 -8.924 26.998 1.00 88.84 A C ANISOU 580 CD GLU A 84 8342 9741 15672 48 1933 -2405 A C ATOM 581 OE1 GLU A 84 -36.105 -8.124 27.125 1.00 90.39 A O ANISOU 581 OE1 GLU A 84 8417 10127 15799 -60 2080 -2515 A O ATOM 582 OE2 GLU A 84 -37.727 -9.021 25.947 1.00 89.90 A O1- ANISOU 582 OE2 GLU A 84 8607 9933 15618 -34 2078 -2485 A O1- ATOM 583 N PRO A 85 -39.519 -11.243 30.428 1.00 65.03 A N ANISOU 583 N PRO A 85 5710 5787 13212 510 871 -1330 A N ATOM 584 CA PRO A 85 -40.266 -10.838 29.235 1.00 64.51 A C ANISOU 584 CA PRO A 85 5785 5880 12844 363 1127 -1414 A C ATOM 585 C PRO A 85 -41.481 -9.971 29.542 1.00 59.19 A C ANISOU 585 C PRO A 85 5420 5279 11788 225 1169 -1043 A C ATOM 586 O PRO A 85 -42.119 -10.146 30.578 1.00 55.77 A O ANISOU 586 O PRO A 85 5107 4707 11377 254 964 -724 A O ATOM 587 CB PRO A 85 -40.706 -12.175 28.648 1.00 64.63 A C ANISOU 587 CB PRO A 85 5759 5690 13109 471 1017 -1580 A C ATOM 588 CG PRO A 85 -40.948 -13.017 29.864 1.00 65.79 A C ANISOU 588 CG PRO A 85 5942 5529 13527 601 674 -1319 A C ATOM 589 CD PRO A 85 -39.944 -12.570 30.910 1.00 66.36 A C ANISOU 589 CD PRO A 85 5896 5625 13694 663 568 -1235 A C ATOM 590 N GLN A 86 -41.790 -9.046 28.636 1.00 62.75 A N ANISOU 590 N GLN A 86 6003 5953 11888 74 1426 -1099 A N ATOM 591 CA GLN A 86 -42.930 -8.149 28.784 1.00 63.28 A C ANISOU 591 CA GLN A 86 6356 6103 11585 -35 1466 -801 A C ATOM 592 C GLN A 86 -44.258 -8.805 28.418 1.00 65.47 A C ANISOU 592 C GLN A 86 6774 6287 11815 -18 1389 -726 A C ATOM 593 O GLN A 86 -45.297 -8.140 28.482 1.00 64.01 A O ANISOU 593 O GLN A 86 6808 6180 11334 -88 1406 -516 A O ATOM 594 CB GLN A 86 -42.692 -6.879 27.965 1.00 65.01 A C ANISOU 594 CB GLN A 86 6687 6567 11446 -195 1742 -884 A C ATOM 595 CG GLN A 86 -41.660 -5.973 28.624 1.00 68.99 A C ANISOU 595 CG GLN A 86 7120 7167 11928 -255 1800 -851 A C ATOM 596 CD GLN A 86 -40.889 -5.124 27.637 1.00 74.34 A C ANISOU 596 CD GLN A 86 7794 8059 12394 -422 2093 -1080 A C ATOM 597 NE2 GLN A 86 -39.860 -5.709 27.032 1.00 76.55 A N ANISOU 597 NE2 GLN A 86 7810 8392 12883 -411 2194 -1439 A N ATOM 598 OE1 GLN A 86 -41.205 -3.951 27.429 1.00 75.37 A O ANISOU 598 OE1 GLN A 86 8159 8302 12174 -567 2224 -944 A O ATOM 599 N ARG A 87 -44.249 -10.085 28.053 1.00 69.88 A N ANISOU 599 N ARG A 87 7204 6681 12667 77 1296 -910 A N ATOM 600 CA ARG A 87 -45.461 -10.858 27.825 1.00 72.89 A C ANISOU 600 CA ARG A 87 7690 6945 13061 88 1198 -849 A C ATOM 601 C ARG A 87 -45.520 -11.968 28.863 1.00 76.28 A C ANISOU 601 C ARG A 87 8058 7085 13838 185 920 -706 A C ATOM 602 O ARG A 87 -44.485 -12.531 29.234 1.00 78.91 A O ANISOU 602 O ARG A 87 8213 7280 14490 295 811 -816 A O ATOM 603 CB ARG A 87 -45.486 -11.472 26.422 1.00 79.64 A C ANISOU 603 CB ARG A 87 8472 7832 13955 97 1324 -1201 A C ATOM 604 CG ARG A 87 -45.873 -10.527 25.309 1.00 83.19 A C ANISOU 604 CG ARG A 87 9066 8544 13997 -21 1565 -1289 A C ATOM 605 CD ARG A 87 -45.646 -11.192 23.964 1.00 88.20 A C ANISOU 605 CD ARG A 87 9587 9229 14696 -12 1692 -1677 A C ATOM 606 NE ARG A 87 -46.013 -10.325 22.851 1.00 91.98 A N ANISOU 606 NE ARG A 87 10229 9960 14759 -133 1910 -1755 A N ATOM 607 CZ ARG A 87 -45.340 -9.232 22.507 1.00 94.77 A C ANISOU 607 CZ ARG A 87 10638 10516 14854 -245 2108 -1784 A C ATOM 608 NH1 ARG A 87 -44.272 -8.867 23.203 1.00 95.60 A N1+ ANISOU 608 NH1 ARG A 87 10619 10619 15086 -251 2125 -1762 A N1+ ATOM 609 NH2 ARG A 87 -45.738 -8.500 21.476 1.00 95.05 A N ANISOU 609 NH2 ARG A 87 10864 10752 14499 -360 2280 -1833 A N ATOM 610 N LEU A 88 -46.724 -12.291 29.329 1.00 72.81 A N ANISOU 610 N LEU A 88 7771 6556 13337 139 797 -470 A N ATOM 611 CA LEU A 88 -46.846 -13.362 30.307 1.00 70.50 A C ANISOU 611 CA LEU A 88 7467 5976 13345 189 533 -305 A C ATOM 612 C LEU A 88 -48.257 -13.934 30.281 1.00 67.66 A C ANISOU 612 C LEU A 88 7248 5540 12919 100 467 -183 A C ATOM 613 O LEU A 88 -49.234 -13.212 30.059 1.00 68.07 A O ANISOU 613 O LEU A 88 7427 5792 12643 1 576 -95 A O ATOM 614 CB LEU A 88 -46.489 -12.872 31.717 1.00 67.79 A C ANISOU 614 CB LEU A 88 7154 5620 12983 187 401 -2 A C ATOM 615 CG LEU A 88 -46.410 -13.928 32.823 1.00 67.28 A C ANISOU 615 CG LEU A 88 7096 5273 13193 235 107 192 A C ATOM 616 CD1 LEU A 88 -45.241 -14.871 32.571 1.00 70.64 A C ANISOU 616 CD1 LEU A 88 7336 5549 13955 393 -13 -62 A C ATOM 617 CD2 LEU A 88 -46.271 -13.270 34.184 1.00 63.51 A C ANISOU 617 CD2 LEU A 88 6684 4891 12557 194 4 507 A C ATOM 618 N GLN A 89 -48.346 -15.240 30.521 1.00 66.83 A N ANISOU 618 N GLN A 89 7119 5135 13139 137 274 -189 A N ATOM 619 CA GLN A 89 -49.614 -15.944 30.645 1.00 61.96 A C ANISOU 619 CA GLN A 89 6626 4449 12467 25 186 -66 A C ATOM 620 C GLN A 89 -49.518 -16.898 31.823 1.00 60.04 A C ANISOU 620 C GLN A 89 6434 4065 12315 19 -83 162 A C ATOM 621 O GLN A 89 -48.496 -17.567 32.003 1.00 61.09 A O ANISOU 621 O GLN A 89 6472 4056 12684 142 -223 77 A O ATOM 622 CB GLN A 89 -49.949 -16.738 29.373 1.00 66.05 A C ANISOU 622 CB GLN A 89 7089 4886 13122 45 252 -388 A C ATOM 623 CG GLN A 89 -51.278 -17.486 29.425 1.00 69.82 A C ANISOU 623 CG GLN A 89 7679 5301 13551 -87 174 -296 A C ATOM 624 CD GLN A 89 -51.713 -18.011 28.069 1.00 73.50 A C ANISOU 624 CD GLN A 89 8090 5737 14100 -82 279 -637 A C ATOM 625 NE2 GLN A 89 -50.742 -18.309 27.212 1.00 75.75 A N ANISOU 625 NE2 GLN A 89 8226 5995 14561 55 334 -959 A N ATOM 626 OE1 GLN A 89 -52.904 -18.172 27.804 1.00 74.54 A O ANISOU 626 OE1 GLN A 89 8296 5913 14112 -204 307 -630 A O ATOM 627 N PHE A 90 -50.579 -16.961 32.621 1.00 57.37 A N ANISOU 627 N PHE A 90 6248 3772 11778 -130 -153 433 A N ATOM 628 CA PHE A 90 -50.601 -17.838 33.783 1.00 58.80 A C ANISOU 628 CA PHE A 90 6525 3828 11987 -173 -386 662 A C ATOM 629 C PHE A 90 -52.049 -18.071 34.186 1.00 59.87 A C ANISOU 629 C PHE A 90 6816 4019 11914 -376 -390 839 A C ATOM 630 O PHE A 90 -52.921 -17.245 33.888 1.00 59.50 A O ANISOU 630 O PHE A 90 6788 4165 11656 -471 -233 847 A O ATOM 631 CB PHE A 90 -49.794 -17.245 34.950 1.00 57.32 A C ANISOU 631 CB PHE A 90 6341 3716 11722 -130 -478 868 A C ATOM 632 CG PHE A 90 -50.227 -15.869 35.354 1.00 54.49 A C ANISOU 632 CG PHE A 90 6022 3627 11054 -210 -339 1019 A C ATOM 633 CD1 PHE A 90 -51.272 -15.696 36.243 1.00 53.77 A C ANISOU 633 CD1 PHE A 90 6070 3672 10689 -373 -366 1257 A C ATOM 634 CD2 PHE A 90 -49.578 -14.750 34.860 1.00 52.97 A C ANISOU 634 CD2 PHE A 90 5730 3555 10841 -129 -178 906 A C ATOM 635 CE1 PHE A 90 -51.671 -14.432 36.625 1.00 51.59 A C ANISOU 635 CE1 PHE A 90 5819 3656 10127 -432 -253 1367 A C ATOM 636 CE2 PHE A 90 -49.974 -13.482 35.237 1.00 49.53 A C ANISOU 636 CE2 PHE A 90 5348 3356 10117 -199 -63 1045 A C ATOM 637 CZ PHE A 90 -51.022 -13.323 36.121 1.00 48.26 A C ANISOU 637 CZ PHE A 90 5312 3339 9687 -338 -110 1268 A C ATOM 638 N PRO A 91 -52.336 -19.178 34.862 1.00 59.19 A N ANISOU 638 N PRO A 91 6842 3766 11880 -455 -566 972 A N ATOM 639 CA PRO A 91 -53.712 -19.452 35.285 1.00 60.27 A C ANISOU 639 CA PRO A 91 7120 3959 11820 -681 -555 1123 A C ATOM 640 C PRO A 91 -54.094 -18.697 36.553 1.00 59.79 A C ANISOU 640 C PRO A 91 7151 4115 11450 -802 -559 1398 A C ATOM 641 O PRO A 91 -53.253 -18.298 37.361 1.00 57.41 A O ANISOU 641 O PRO A 91 6847 3855 11113 -720 -636 1523 A O ATOM 642 CB PRO A 91 -53.715 -20.967 35.526 1.00 56.74 A C ANISOU 642 CB PRO A 91 6775 3221 11563 -721 -737 1149 A C ATOM 643 CG PRO A 91 -52.296 -21.312 35.828 1.00 58.40 A C ANISOU 643 CG PRO A 91 6934 3265 11989 -521 -900 1136 A C ATOM 644 CD PRO A 91 -51.410 -20.277 35.191 1.00 56.16 A C ANISOU 644 CD PRO A 91 6463 3121 11755 -345 -779 962 A C ATOM 645 N LEU A 92 -55.409 -18.522 36.716 1.00 52.73 A N ANISOU 645 N LEU A 92 6131 3881 10022 17 229 2014 A N ATOM 646 CA LEU A 92 -55.959 -17.872 37.896 1.00 53.26 A C ANISOU 646 CA LEU A 92 6221 4156 9858 -110 141 2121 A C ATOM 647 C LEU A 92 -55.645 -18.666 39.157 1.00 58.60 A C ANISOU 647 C LEU A 92 6893 4757 10615 -227 -77 2332 A C ATOM 648 O LEU A 92 -55.413 -19.877 39.104 1.00 61.87 A O ANISOU 648 O LEU A 92 7314 5036 11156 -227 -170 2346 A O ATOM 649 CB LEU A 92 -57.475 -17.712 37.783 1.00 45.45 A C ANISOU 649 CB LEU A 92 5318 3346 8603 -205 198 2055 A C ATOM 650 CG LEU A 92 -58.111 -16.322 37.685 1.00 48.30 A C ANISOU 650 CG LEU A 92 5690 3941 8722 -201 301 1944 A C ATOM 651 CD1 LEU A 92 -57.439 -15.448 36.658 1.00 44.53 A C ANISOU 651 CD1 LEU A 92 5188 3433 8297 -44 437 1808 A C ATOM 652 CD2 LEU A 92 -59.600 -16.450 37.397 1.00 51.10 A C ANISOU 652 CD2 LEU A 92 6114 4414 8888 -278 346 1856 A C ATOM 653 N PRO A 93 -55.632 -18.001 40.309 1.00 63.11 A N ANISOU 653 N PRO A 93 7463 5478 11039 -330 -167 2441 A N ATOM 654 CA PRO A 93 -55.464 -18.734 41.563 1.00 65.81 A C ANISOU 654 CA PRO A 93 7836 5797 11371 -473 -384 2617 A C ATOM 655 C PRO A 93 -56.676 -19.611 41.816 1.00 68.77 A C ANISOU 655 C PRO A 93 8319 6195 11616 -638 -428 2671 A C ATOM 656 O PRO A 93 -57.799 -19.297 41.411 1.00 69.86 A O ANISOU 656 O PRO A 93 8498 6469 11577 -681 -299 2574 A O ATOM 657 CB PRO A 93 -55.349 -17.624 42.614 1.00 63.86 A C ANISOU 657 CB PRO A 93 7577 5721 10965 -564 -426 2709 A C ATOM 658 CG PRO A 93 -56.066 -16.459 42.003 1.00 60.38 A C ANISOU 658 CG PRO A 93 7130 5484 10329 -515 -225 2538 A C ATOM 659 CD PRO A 93 -55.803 -16.554 40.525 1.00 59.42 A C ANISOU 659 CD PRO A 93 6976 5237 10363 -327 -77 2376 A C ATOM 660 N THR A 94 -56.439 -20.720 42.504 1.00 72.94 A N ANISOU 660 N THR A 94 8893 6638 12184 -723 -613 2772 A N ATOM 661 CA THR A 94 -57.482 -21.684 42.804 1.00 77.88 A C ANISOU 661 CA THR A 94 9630 7268 12691 -890 -672 2827 A C ATOM 662 C THR A 94 -57.472 -21.958 44.301 1.00 81.13 A C ANISOU 662 C THR A 94 10120 7753 12953 -1095 -867 2987 A C ATOM 663 O THR A 94 -56.567 -21.537 45.026 1.00 82.33 A O ANISOU 663 O THR A 94 10234 7919 13130 -1084 -974 3055 A O ATOM 664 CB THR A 94 -57.284 -22.978 42.001 1.00 83.26 A C ANISOU 664 CB THR A 94 10318 7746 13572 -795 -697 2771 A C ATOM 665 CG2 THR A 94 -58.546 -23.815 42.030 1.00 85.96 A C ANISOU 665 CG2 THR A 94 10773 8105 13782 -952 -700 2794 A C ATOM 666 OG1 THR A 94 -57.010 -22.645 40.635 1.00 84.69 A O ANISOU 666 OG1 THR A 94 10421 7856 13902 -595 -517 2607 A O ATOM 667 N ALA A 95 -58.498 -22.668 44.771 1.00 90.63 A N ANISOU 667 N ALA A 95 11439 9006 13990 -1293 -912 3040 A N ATOM 668 CA ALA A 95 -58.461 -23.162 46.142 1.00 94.07 A C ANISOU 668 CA ALA A 95 11974 9482 14285 -1496 -1107 3182 A C ATOM 669 C ALA A 95 -57.293 -24.116 46.362 1.00 98.13 A C ANISOU 669 C ALA A 95 12475 9788 15020 -1409 -1314 3253 A C ATOM 670 O ALA A 95 -56.714 -24.148 47.454 1.00 97.22 A O ANISOU 670 O ALA A 95 12393 9686 14861 -1501 -1493 3367 A O ATOM 671 CB ALA A 95 -59.784 -23.843 46.491 1.00 89.32 A C ANISOU 671 CB ALA A 95 11501 8961 13473 -1725 -1098 3201 A C ATOM 672 N GLN A 96 -56.927 -24.891 45.339 1.00106.02 A N ANISOU 672 N GLN A 96 13422 10598 16262 -1237 -1296 3178 A N ATOM 673 CA GLN A 96 -55.800 -25.815 45.418 1.00110.73 A C ANISOU 673 CA GLN A 96 13976 10989 17107 -1140 -1481 3217 A C ATOM 674 C GLN A 96 -54.473 -25.064 45.388 1.00107.62 A C ANISOU 674 C GLN A 96 13439 10560 16893 -978 -1503 3191 A C ATOM 675 O GLN A 96 -53.741 -25.038 46.383 1.00110.59 A O ANISOU 675 O GLN A 96 13812 10926 17281 -1035 -1692 3298 A O ATOM 676 CB GLN A 96 -55.845 -26.835 44.273 1.00112.76 A C ANISOU 676 CB GLN A 96 14207 11069 17569 -1011 -1429 3118 A C ATOM 677 CG GLN A 96 -57.181 -27.575 44.087 1.00117.97 A C ANISOU 677 CG GLN A 96 14996 11753 18075 -1150 -1378 3119 A C ATOM 678 CD GLN A 96 -58.287 -26.691 43.523 1.00117.80 A C ANISOU 678 CD GLN A 96 14987 11898 17875 -1181 -1145 3031 A C ATOM 679 NE2 GLN A 96 -58.806 -27.057 42.358 1.00116.75 A N ANISOU 679 NE2 GLN A 96 14843 11697 17818 -1094 -1003 2912 A N ATOM 680 OE1 GLN A 96 -58.665 -25.692 44.129 1.00117.62 A O ANISOU 680 OE1 GLN A 96 14977 12060 17653 -1287 -1098 3063 A O ATOM 681 N ARG A 97 -54.155 -24.452 44.250 1.00 91.93 A N ANISOU 681 N ARG A 97 11334 8552 15042 -785 -1311 3043 A N ATOM 682 CA ARG A 97 -52.914 -23.711 44.068 1.00 84.90 A C ANISOU 682 CA ARG A 97 10298 7630 14329 -626 -1294 2989 A C ATOM 683 C ARG A 97 -53.211 -22.221 43.982 1.00 81.68 A C ANISOU 683 C ARG A 97 9868 7408 13758 -616 -1120 2949 A C ATOM 684 O ARG A 97 -54.118 -21.804 43.253 1.00 83.56 A O ANISOU 684 O ARG A 97 10135 7726 13888 -607 -930 2866 A O ATOM 685 CB ARG A 97 -52.188 -24.185 42.806 1.00 80.46 A C ANISOU 685 CB ARG A 97 9615 6896 14062 -418 -1201 2830 A C ATOM 686 CG ARG A 97 -51.017 -23.319 42.376 1.00 75.85 A C ANISOU 686 CG ARG A 97 8873 6297 13650 -255 -1117 2729 A C ATOM 687 CD ARG A 97 -50.420 -23.817 41.066 1.00 73.59 A C ANISOU 687 CD ARG A 97 8477 5858 13626 -82 -992 2546 A C ATOM 688 N SER A 98 -52.449 -21.427 44.728 1.00 78.60 A N ANISOU 688 N SER A 98 9426 7081 13358 -621 -1194 3009 A N ATOM 689 CA SER A 98 -52.561 -19.978 44.711 1.00 73.14 A C ANISOU 689 CA SER A 98 8700 6556 12533 -602 -1048 2976 A C ATOM 690 C SER A 98 -51.356 -19.370 44.005 1.00 66.99 A C ANISOU 690 C SER A 98 7769 5706 11979 -398 -962 2863 A C ATOM 691 O SER A 98 -50.275 -19.965 43.956 1.00 62.15 A O ANISOU 691 O SER A 98 7066 4939 11608 -311 -1069 2847 A O ATOM 692 CB SER A 98 -52.677 -19.420 46.133 1.00 75.86 A C ANISOU 692 CB SER A 98 9109 7054 12660 -784 -1176 3121 A C ATOM 693 OG SER A 98 -53.956 -19.690 46.681 1.00 78.43 A O ANISOU 693 OG SER A 98 9573 7499 12726 -993 -1184 3185 A O ATOM 694 N LEU A 99 -51.556 -18.177 43.452 1.00 64.37 A N ANISOU 694 N LEU A 99 7405 5484 11567 -331 -766 2777 A N ATOM 695 CA LEU A 99 -50.473 -17.475 42.778 1.00 66.50 A C ANISOU 695 CA LEU A 99 7545 5708 12014 -158 -659 2659 A C ATOM 696 C LEU A 99 -49.277 -17.289 43.705 1.00 69.75 A C ANISOU 696 C LEU A 99 7875 6095 12533 -159 -831 2742 A C ATOM 697 O LEU A 99 -49.411 -17.195 44.928 1.00 72.20 A O ANISOU 697 O LEU A 99 8245 6488 12701 -303 -993 2893 A O ATOM 698 CB LEU A 99 -50.955 -16.121 42.261 1.00 61.12 A C ANISOU 698 CB LEU A 99 6870 5171 11182 -118 -449 2582 A C ATOM 699 CG LEU A 99 -51.838 -16.199 41.015 1.00 57.64 A C ANISOU 699 CG LEU A 99 6479 4716 10706 -62 -253 2449 A C ATOM 700 CD1 LEU A 99 -52.049 -14.817 40.421 1.00 45.78 A C ANISOU 700 CD1 LEU A 99 4973 3324 9099 3 -59 2356 A C ATOM 701 CD2 LEU A 99 -51.226 -17.142 39.992 1.00 58.66 A C ANISOU 701 CD2 LEU A 99 6552 4660 11074 60 -209 2320 A C ATOM 702 N GLU A 100 -48.091 -17.238 43.099 1.00 72.05 A N ANISOU 702 N GLU A 100 8028 6272 13075 -9 -788 2631 A N ATOM 703 CA GLU A 100 -46.830 -17.067 43.799 1.00 74.48 A C ANISOU 703 CA GLU A 100 8230 6532 13537 12 -936 2678 A C ATOM 704 C GLU A 100 -45.981 -16.038 43.065 1.00 71.19 A C ANISOU 704 C GLU A 100 7690 6128 13231 151 -755 2536 A C ATOM 705 O GLU A 100 -45.961 -16.023 41.825 1.00 70.19 A O ANISOU 705 O GLU A 100 7527 5951 13191 258 -555 2368 A O ATOM 706 CB GLU A 100 -46.059 -18.389 43.918 1.00 85.28 A C ANISOU 706 CB GLU A 100 9532 7704 15168 34 -1120 2686 A C ATOM 707 CG GLU A 100 -46.578 -19.312 45.009 1.00 93.17 A C ANISOU 707 CG GLU A 100 10651 8687 16064 -126 -1366 2863 A C ATOM 708 CD GLU A 100 -46.468 -18.690 46.387 1.00 98.88 A C ANISOU 708 CD GLU A 100 11425 9527 16617 -262 -1530 3026 A C ATOM 709 OE1 GLU A 100 -45.621 -17.789 46.565 1.00101.08 A O ANISOU 709 OE1 GLU A 100 11606 9842 16958 -205 -1514 3006 A O ATOM 710 OE2 GLU A 100 -47.233 -19.093 47.289 1.00101.47 A O1- ANISOU 710 OE2 GLU A 100 11896 9916 16741 -435 -1668 3167 A O1- ATOM 711 N PRO A 101 -45.279 -15.170 43.791 1.00 66.89 A N ANISOU 711 N PRO A 101 7089 5650 12675 140 -818 2593 A N ATOM 712 CA PRO A 101 -44.366 -14.222 43.133 1.00 64.76 A C ANISOU 712 CA PRO A 101 6699 5383 12525 263 -654 2456 A C ATOM 713 C PRO A 101 -43.267 -14.966 42.391 1.00 67.05 A C ANISOU 713 C PRO A 101 6845 5488 13145 371 -636 2312 A C ATOM 714 O PRO A 101 -42.507 -15.737 42.982 1.00 68.77 A O ANISOU 714 O PRO A 101 6987 5588 13554 357 -840 2365 A O ATOM 715 CB PRO A 101 -43.812 -13.396 44.300 1.00 64.42 A C ANISOU 715 CB PRO A 101 6629 5431 12418 203 -788 2579 A C ATOM 716 CG PRO A 101 -43.971 -14.280 45.495 1.00 66.57 A C ANISOU 716 CG PRO A 101 6965 5673 12656 70 -1064 2755 A C ATOM 717 CD PRO A 101 -45.224 -15.068 45.259 1.00 67.37 A C ANISOU 717 CD PRO A 101 7198 5782 12619 3 -1046 2782 A C ATOM 718 N GLY A 102 -43.185 -14.729 41.084 1.00 67.96 A N ANISOU 718 N GLY A 102 6924 5576 13324 470 -391 2122 A N ATOM 719 CA GLY A 102 -42.177 -15.353 40.248 1.00 75.44 A C ANISOU 719 CA GLY A 102 7731 6362 14571 559 -327 1951 A C ATOM 720 C GLY A 102 -41.545 -14.349 39.303 1.00 74.91 A C ANISOU 720 C GLY A 102 7593 6324 14547 638 -77 1769 A C ATOM 721 O GLY A 102 -41.226 -13.221 39.676 1.00 71.78 A O ANISOU 721 O GLY A 102 7181 6027 14066 638 -45 1797 A O ATOM 722 N THR A 103 -41.361 -14.779 38.056 1.00 79.94 A N ANISOU 722 N THR A 103 8192 6871 15310 695 107 1576 A N ATOM 723 CA THR A 103 -40.777 -13.946 37.019 1.00 80.48 A C ANISOU 723 CA THR A 103 8212 6954 15413 748 365 1379 A C ATOM 724 C THR A 103 -41.738 -13.792 35.846 1.00 79.75 A C ANISOU 724 C THR A 103 8257 6902 15141 752 593 1268 A C ATOM 725 O THR A 103 -42.485 -14.721 35.525 1.00 81.25 A O ANISOU 725 O THR A 103 8516 7043 15312 739 573 1273 A O ATOM 726 CB THR A 103 -39.459 -14.546 36.514 1.00 85.39 A C ANISOU 726 CB THR A 103 8649 7422 16372 790 398 1210 A C ATOM 727 CG2 THR A 103 -39.648 -16.018 36.167 1.00 88.61 A C ANISOU 727 CG2 THR A 103 9036 7692 16938 795 329 1174 A C ATOM 728 OG1 THR A 103 -39.023 -13.840 35.346 1.00 87.43 A O ANISOU 728 OG1 THR A 103 8887 7693 16637 815 682 998 A O ATOM 729 N PRO A 104 -41.744 -12.625 35.183 1.00 76.94 A N ANISOU 729 N PRO A 104 7955 6632 14648 766 805 1167 A N ATOM 730 CA PRO A 104 -40.903 -11.449 35.448 1.00 75.22 A C ANISOU 730 CA PRO A 104 7669 6476 14434 780 857 1146 A C ATOM 731 C PRO A 104 -41.323 -10.681 36.701 1.00 72.35 A C ANISOU 731 C PRO A 104 7353 6243 13892 751 697 1356 A C ATOM 732 O PRO A 104 -42.447 -10.852 37.171 1.00 72.52 A O ANISOU 732 O PRO A 104 7492 6331 13730 711 601 1493 A O ATOM 733 CB PRO A 104 -41.093 -10.597 34.191 1.00 73.07 A C ANISOU 733 CB PRO A 104 7494 6247 14022 786 1142 972 A C ATOM 734 CG PRO A 104 -42.452 -10.944 33.720 1.00 73.10 A C ANISOU 734 CG PRO A 104 7667 6278 13830 766 1177 994 A C ATOM 735 CD PRO A 104 -42.642 -12.405 34.036 1.00 75.84 A C ANISOU 735 CD PRO A 104 7966 6526 14325 760 1014 1056 A C ATOM 736 N ARG A 105 -40.421 -9.851 37.235 1.00 69.64 A N ANISOU 736 N ARG A 105 6919 5938 13603 761 672 1373 A N ATOM 737 CA ARG A 105 -40.719 -9.132 38.471 1.00 67.74 A C ANISOU 737 CA ARG A 105 6713 5821 13204 725 515 1568 A C ATOM 738 C ARG A 105 -41.956 -8.257 38.317 1.00 64.38 A C ANISOU 738 C ARG A 105 6457 5539 12467 705 611 1614 A C ATOM 739 O ARG A 105 -42.781 -8.172 39.235 1.00 65.03 A O ANISOU 739 O ARG A 105 6614 5716 12380 647 468 1787 A O ATOM 740 CB ARG A 105 -39.518 -8.282 38.889 1.00 70.26 A C ANISOU 740 CB ARG A 105 6909 6158 13628 743 509 1550 A C ATOM 741 CG ARG A 105 -38.470 -9.020 39.711 1.00 74.49 A C ANISOU 741 CG ARG A 105 7291 6587 14424 735 294 1605 A C ATOM 742 CD ARG A 105 -37.079 -8.843 39.122 1.00 75.87 A C ANISOU 742 CD ARG A 105 7307 6670 14852 779 410 1418 A C ATOM 743 NE ARG A 105 -36.778 -7.449 38.804 1.00 76.26 A N ANISOU 743 NE ARG A 105 7371 6819 14785 793 592 1344 A N ATOM 744 CZ ARG A 105 -35.692 -7.055 38.146 1.00 76.73 A C ANISOU 744 CZ ARG A 105 7324 6826 15003 814 750 1160 A C ATOM 745 NH1 ARG A 105 -34.805 -7.951 37.738 1.00 80.06 A N1+ ANISOU 745 NH1 ARG A 105 7607 7098 15715 825 751 1025 A N1+ ATOM 746 NH2 ARG A 105 -35.492 -5.768 37.894 1.00 74.17 A N ANISOU 746 NH2 ARG A 105 7035 6600 14547 817 909 1103 A N ATOM 747 N TRP A 106 -42.104 -7.595 37.167 1.00 61.12 A N ANISOU 747 N TRP A 106 6112 5141 11969 739 848 1455 A N ATOM 748 CA TRP A 106 -43.221 -6.672 36.991 1.00 58.66 A C ANISOU 748 CA TRP A 106 5961 4955 11374 725 930 1485 A C ATOM 749 C TRP A 106 -44.566 -7.377 37.108 1.00 53.21 A C ANISOU 749 C TRP A 106 5385 4293 10540 677 851 1570 A C ATOM 750 O TRP A 106 -45.543 -6.770 37.562 1.00 48.92 A O ANISOU 750 O TRP A 106 4944 3932 9714 617 807 1636 A O ATOM 751 CB TRP A 106 -43.107 -5.946 35.649 1.00 59.71 A C ANISOU 751 CB TRP A 106 6172 5090 11427 750 1183 1281 A C ATOM 752 CG TRP A 106 -43.268 -6.826 34.445 1.00 62.26 A C ANISOU 752 CG TRP A 106 6535 5285 11835 760 1316 1132 A C ATOM 753 CD1 TRP A 106 -42.269 -7.401 33.721 1.00 64.17 A C ANISOU 753 CD1 TRP A 106 6677 5409 12297 772 1420 973 A C ATOM 754 CD2 TRP A 106 -44.496 -7.225 33.820 1.00 62.37 A C ANISOU 754 CD2 TRP A 106 6702 5309 11688 736 1355 1111 A C ATOM 755 CE2 TRP A 106 -44.159 -8.043 32.723 1.00 63.39 A C ANISOU 755 CE2 TRP A 106 6821 5308 11956 742 1486 947 A C ATOM 756 CE3 TRP A 106 -45.846 -6.973 34.082 1.00 61.06 A C ANISOU 756 CE3 TRP A 106 6673 5293 11233 687 1281 1191 A C ATOM 757 NE1 TRP A 106 -42.793 -8.133 32.683 1.00 64.60 A N ANISOU 757 NE1 TRP A 106 6815 5393 12336 759 1527 860 A N ATOM 758 CZ2 TRP A 106 -45.121 -8.610 31.889 1.00 63.02 A C ANISOU 758 CZ2 TRP A 106 6907 5230 11810 721 1551 887 A C ATOM 759 CZ3 TRP A 106 -46.800 -7.536 33.252 1.00 60.83 A C ANISOU 759 CZ3 TRP A 106 6766 5236 11112 669 1339 1125 A C ATOM 760 CH2 TRP A 106 -46.432 -8.345 32.169 1.00 61.50 A C ANISOU 760 CH2 TRP A 106 6847 5147 11371 693 1474 985 A C ATOM 761 N ALA A 107 -44.643 -8.651 36.715 1.00 54.36 A N ANISOU 761 N ALA A 107 5512 4317 10825 679 827 1532 A N ATOM 762 CA ALA A 107 -45.911 -9.365 36.807 1.00 54.78 A C ANISOU 762 CA ALA A 107 5671 4385 10756 631 758 1610 A C ATOM 763 C ALA A 107 -46.318 -9.630 38.250 1.00 56.04 A C ANISOU 763 C ALA A 107 5825 4614 10854 552 526 1826 A C ATOM 764 O ALA A 107 -47.484 -9.953 38.502 1.00 58.58 A O ANISOU 764 O ALA A 107 6246 4998 11014 483 472 1902 A O ATOM 765 CB ALA A 107 -45.834 -10.686 36.042 1.00 54.67 A C ANISOU 765 CB ALA A 107 5638 4229 10906 647 784 1511 A C ATOM 766 N ASN A 108 -45.386 -9.505 39.197 1.00 56.30 A N ANISOU 766 N ASN A 108 5750 4648 10992 542 388 1915 A N ATOM 767 CA ASN A 108 -45.727 -9.706 40.601 1.00 55.24 A C ANISOU 767 CA ASN A 108 5632 4586 10772 440 165 2120 A C ATOM 768 C ASN A 108 -46.756 -8.690 41.078 1.00 49.88 A C ANISOU 768 C ASN A 108 5058 4110 9786 366 188 2189 A C ATOM 769 O ASN A 108 -47.592 -9.008 41.932 1.00 46.49 A O ANISOU 769 O ASN A 108 4695 3768 9203 248 62 2314 A O ATOM 770 CB ASN A 108 -44.466 -9.622 41.461 1.00 58.99 A C ANISOU 770 CB ASN A 108 5979 5028 11404 442 19 2184 A C ATOM 771 CG ASN A 108 -43.510 -10.771 41.211 1.00 63.66 A C ANISOU 771 CG ASN A 108 6457 5440 12289 487 -53 2119 A C ATOM 772 ND2 ASN A 108 -42.224 -10.530 41.443 1.00 63.97 A N ANISOU 772 ND2 ASN A 108 6361 5426 12520 528 -95 2086 A N ATOM 773 OD1 ASN A 108 -43.921 -11.860 40.811 1.00 67.17 A O ANISOU 773 OD1 ASN A 108 6932 5794 12796 483 -73 2093 A O ATOM 774 N TYR A 109 -46.707 -7.466 40.548 1.00 41.82 A N ANISOU 774 N TYR A 109 4054 3209 8625 410 347 2065 A N ATOM 775 CA TYR A 109 -47.630 -6.427 40.994 1.00 45.92 A C ANISOU 775 CA TYR A 109 4658 3965 8825 338 363 2072 A C ATOM 776 C TYR A 109 -49.073 -6.763 40.629 1.00 48.58 A C ANISOU 776 C TYR A 109 5108 4378 8972 286 400 2029 A C ATOM 777 O TYR A 109 -49.978 -6.602 41.456 1.00 48.03 A O ANISOU 777 O TYR A 109 5085 4461 8704 177 323 2100 A O ATOM 778 CB TYR A 109 -47.204 -5.072 40.424 1.00 39.25 A C ANISOU 778 CB TYR A 109 3813 3203 7898 405 513 1945 A C ATOM 779 CG TYR A 109 -45.891 -4.575 40.997 1.00 48.87 A C ANISOU 779 CG TYR A 109 4917 4390 9259 434 466 1996 A C ATOM 780 CD1 TYR A 109 -44.675 -4.993 40.472 1.00 48.37 A C ANISOU 780 CD1 TYR A 109 4749 4139 9489 520 508 1941 A C ATOM 781 CD2 TYR A 109 -45.871 -3.704 42.080 1.00 48.34 A C ANISOU 781 CD2 TYR A 109 4841 4482 9046 369 379 2090 A C ATOM 782 CE1 TYR A 109 -43.478 -4.550 41.001 1.00 51.63 A C ANISOU 782 CE1 TYR A 109 5044 4521 10051 548 459 1978 A C ATOM 783 CE2 TYR A 109 -44.681 -3.255 42.615 1.00 49.85 A C ANISOU 783 CE2 TYR A 109 4928 4644 9368 393 328 2139 A C ATOM 784 CZ TYR A 109 -43.487 -3.680 42.072 1.00 51.53 A C ANISOU 784 CZ TYR A 109 5033 4668 9879 485 364 2084 A C ATOM 785 OH TYR A 109 -42.298 -3.236 42.602 1.00 50.12 A O ANISOU 785 OH TYR A 109 4739 4457 9848 509 308 2123 A O ATOM 786 N VAL A 110 -49.315 -7.227 39.401 1.00 49.16 A N ANISOU 786 N VAL A 110 5225 4350 9105 351 521 1903 A N ATOM 787 CA VAL A 110 -50.675 -7.595 39.016 1.00 47.02 A C ANISOU 787 CA VAL A 110 5056 4138 8672 305 547 1857 A C ATOM 788 C VAL A 110 -51.085 -8.902 39.683 1.00 40.23 A C ANISOU 788 C VAL A 110 4195 3210 7880 221 405 1989 A C ATOM 789 O VAL A 110 -52.234 -9.062 40.113 1.00 46.71 A O ANISOU 789 O VAL A 110 5079 4149 8521 121 359 2021 A O ATOM 790 CB VAL A 110 -50.799 -7.675 37.483 1.00 47.56 A C ANISOU 790 CB VAL A 110 5187 4114 8770 389 713 1685 A C ATOM 791 CG1 VAL A 110 -50.098 -6.490 36.838 1.00 38.13 A C ANISOU 791 CG1 VAL A 110 3996 2944 7548 459 843 1570 A C ATOM 792 CG2 VAL A 110 -50.239 -8.992 36.965 1.00 52.09 A C ANISOU 792 CG2 VAL A 110 5718 4465 9609 431 719 1680 A C ATOM 793 N LYS A 111 -50.154 -9.856 39.783 1.00 41.66 A N ANISOU 793 N LYS A 111 4303 3196 8330 253 328 2061 A N ATOM 794 CA LYS A 111 -50.452 -11.115 40.458 1.00 42.93 A C ANISOU 794 CA LYS A 111 4475 3269 8569 167 166 2202 A C ATOM 795 C LYS A 111 -50.898 -10.879 41.895 1.00 50.63 A C ANISOU 795 C LYS A 111 5477 4397 9362 15 13 2361 A C ATOM 796 O LYS A 111 -51.874 -11.482 42.358 1.00 49.98 A O ANISOU 796 O LYS A 111 5468 4368 9153 -108 -57 2427 A O ATOM 797 CB LYS A 111 -49.236 -12.041 40.414 1.00 44.63 A C ANISOU 797 CB LYS A 111 4592 3247 9119 235 79 2242 A C ATOM 798 CG LYS A 111 -48.879 -12.541 39.022 1.00 44.94 A C ANISOU 798 CG LYS A 111 4605 3148 9322 350 230 2057 A C ATOM 799 CD LYS A 111 -47.816 -13.628 39.086 1.00 46.92 A C ANISOU 799 CD LYS A 111 4748 3241 9839 387 122 2041 A C ATOM 800 CE LYS A 111 -47.300 -13.983 37.701 1.00 47.35 A C ANISOU 800 CE LYS A 111 4756 3173 10061 489 297 1836 A C ATOM 801 NZ LYS A 111 -46.333 -15.116 37.754 1.00 52.89 A N1+ ANISOU 801 NZ LYS A 111 5341 3717 11038 519 188 1811 A N1+ ATOM 802 N GLY A 112 -50.197 -10.003 42.617 1.00 42.86 A N ANISOU 802 N GLY A 112 4440 3489 8356 8 -33 2417 A N ATOM 803 CA GLY A 112 -50.566 -9.741 43.998 1.00 45.46 A C ANISOU 803 CA GLY A 112 4802 3968 8505 -153 -170 2561 A C ATOM 804 C GLY A 112 -51.961 -9.162 44.136 1.00 45.10 A C ANISOU 804 C GLY A 112 4835 4151 8150 -252 -89 2491 A C ATOM 805 O GLY A 112 -52.732 -9.578 45.004 1.00 42.45 A O ANISOU 805 O GLY A 112 4559 3900 7672 -419 -182 2582 A O ATOM 806 N VAL A 113 -52.305 -8.192 43.284 1.00 40.41 A N ANISOU 806 N VAL A 113 4244 3655 7454 -159 78 2321 A N ATOM 807 CA VAL A 113 -53.644 -7.607 43.323 1.00 42.45 A C ANISOU 807 CA VAL A 113 4559 4115 7455 -232 147 2226 A C ATOM 808 C VAL A 113 -54.694 -8.668 43.014 1.00 44.62 A C ANISOU 808 C VAL A 113 4897 4356 7701 -295 145 2209 A C ATOM 809 O VAL A 113 -55.767 -8.700 43.629 1.00 45.58 A O ANISOU 809 O VAL A 113 5055 4623 7639 -436 123 2210 A O ATOM 810 CB VAL A 113 -53.739 -6.410 42.356 1.00 40.99 A C ANISOU 810 CB VAL A 113 4376 4000 7200 -106 300 2049 A C ATOM 811 CG1 VAL A 113 -55.154 -5.844 42.342 1.00 37.07 A C ANISOU 811 CG1 VAL A 113 3924 3688 6473 -167 350 1935 A C ATOM 812 CG2 VAL A 113 -52.738 -5.330 42.746 1.00 42.39 A C ANISOU 812 CG2 VAL A 113 4496 4224 7388 -62 301 2069 A C ATOM 813 N ILE A 114 -54.401 -9.554 42.060 1.00 44.30 A N ANISOU 813 N ILE A 114 4864 4123 7844 -199 174 2181 A N ATOM 814 CA ILE A 114 -55.327 -10.636 41.737 1.00 46.17 A C ANISOU 814 CA ILE A 114 5161 4309 8072 -255 167 2171 A C ATOM 815 C ILE A 114 -55.552 -11.526 42.954 1.00 46.85 A C ANISOU 815 C ILE A 114 5274 4395 8133 -434 5 2346 A C ATOM 816 O ILE A 114 -56.691 -11.853 43.306 1.00 51.25 A O ANISOU 816 O ILE A 114 5886 5057 8528 -570 -5 2340 A O ATOM 817 CB ILE A 114 -54.804 -11.450 40.540 1.00 47.22 A C ANISOU 817 CB ILE A 114 5292 4219 8431 -122 224 2114 A C ATOM 818 CG1 ILE A 114 -54.788 -10.592 39.274 1.00 44.25 A C ANISOU 818 CG1 ILE A 114 4928 3856 8029 14 393 1930 A C ATOM 819 CG2 ILE A 114 -55.634 -12.713 40.350 1.00 45.38 A C ANISOU 819 CG2 ILE A 114 5118 3911 8213 -191 189 2134 A C ATOM 820 CD1 ILE A 114 -54.233 -11.306 38.069 1.00 40.38 A C ANISOU 820 CD1 ILE A 114 4440 3157 7744 127 475 1852 A C ATOM 821 N GLN A 115 -54.464 -11.927 43.617 1.00 49.03 A N ANISOU 821 N GLN A 115 5516 4547 8568 -446 -132 2501 A N ATOM 822 CA GLN A 115 -54.576 -12.876 44.721 1.00 49.76 A C ANISOU 822 CA GLN A 115 5658 4597 8651 -624 -315 2686 A C ATOM 823 C GLN A 115 -55.426 -12.321 45.855 1.00 49.73 A C ANISOU 823 C GLN A 115 5704 4831 8361 -828 -341 2725 A C ATOM 824 O GLN A 115 -56.187 -13.061 46.490 1.00 52.28 A O ANISOU 824 O GLN A 115 6105 5186 8572 -1014 -416 2801 A O ATOM 825 CB GLN A 115 -53.187 -13.251 45.240 1.00 52.50 A C ANISOU 825 CB GLN A 115 5955 4762 9231 -591 -481 2842 A C ATOM 826 CG GLN A 115 -53.207 -14.254 46.388 1.00 54.87 A C ANISOU 826 CG GLN A 115 6329 5016 9505 -771 -702 3016 A C ATOM 827 CD GLN A 115 -53.616 -15.644 45.937 1.00 57.47 A C ANISOU 827 CD GLN A 115 6712 5202 9922 -778 -747 3006 A C ATOM 828 NE2 GLN A 115 -54.295 -16.378 46.813 1.00 57.00 A N ANISOU 828 NE2 GLN A 115 6761 5189 9708 -981 -870 3104 A N ATOM 829 OE1 GLN A 115 -53.328 -16.052 44.811 1.00 57.56 A O ANISOU 829 OE1 GLN A 115 6674 5068 10129 -612 -664 2902 A O ATOM 830 N TYR A 116 -55.316 -11.022 46.124 1.00 48.41 A N ANISOU 830 N TYR A 116 5492 4832 8070 -810 -273 2662 A N ATOM 831 CA TYR A 116 -55.996 -10.409 47.255 1.00 48.74 A C ANISOU 831 CA TYR A 116 5565 5100 7855 -1006 -290 2684 A C ATOM 832 C TYR A 116 -57.278 -9.688 46.868 1.00 47.09 A C ANISOU 832 C TYR A 116 5350 5092 7449 -1020 -130 2486 A C ATOM 833 O TYR A 116 -57.884 -9.038 47.725 1.00 48.10 A O ANISOU 833 O TYR A 116 5481 5423 7372 -1171 -113 2457 A O ATOM 834 CB TYR A 116 -55.052 -9.433 47.965 1.00 43.53 A C ANISOU 834 CB TYR A 116 4855 4500 7185 -998 -337 2747 A C ATOM 835 CG TYR A 116 -53.836 -10.098 48.560 1.00 45.02 A C ANISOU 835 CG TYR A 116 5044 4503 7558 -1014 -529 2951 A C ATOM 836 CD1 TYR A 116 -53.965 -11.064 49.547 1.00 50.40 A C ANISOU 836 CD1 TYR A 116 5814 5132 8202 -1220 -707 3131 A C ATOM 837 CD2 TYR A 116 -52.560 -9.770 48.126 1.00 44.81 A C ANISOU 837 CD2 TYR A 116 4931 4343 7752 -831 -540 2957 A C ATOM 838 CE1 TYR A 116 -52.860 -11.680 50.089 1.00 53.32 A C ANISOU 838 CE1 TYR A 116 6187 5348 8725 -1208 -906 3257 A C ATOM 839 CE2 TYR A 116 -51.446 -10.381 48.663 1.00 50.26 A C ANISOU 839 CE2 TYR A 116 5604 4851 8643 -836 -732 3130 A C ATOM 840 CZ TYR A 116 -51.603 -11.336 49.645 1.00 54.88 A C ANISOU 840 CZ TYR A 116 6276 5422 9153 -1008 -920 3240 A C ATOM 841 OH TYR A 116 -50.504 -11.954 50.193 1.00 56.63 A O ANISOU 841 OH TYR A 116 6478 5508 9531 -990 -1122 3322 A O ATOM 842 N TYR A 117 -57.706 -9.777 45.614 1.00 45.21 A N ANISOU 842 N TYR A 117 5104 4800 7274 -873 -18 2340 A N ATOM 843 CA TYR A 117 -58.955 -9.136 45.233 1.00 44.97 A C ANISOU 843 CA TYR A 117 5067 4940 7078 -882 104 2150 A C ATOM 844 C TYR A 117 -60.097 -9.766 46.024 1.00 47.45 A C ANISOU 844 C TYR A 117 5427 5368 7235 -1113 76 2164 A C ATOM 845 O TYR A 117 -60.207 -11.000 46.069 1.00 47.39 A O ANISOU 845 O TYR A 117 5478 5242 7287 -1189 6 2263 A O ATOM 846 CB TYR A 117 -59.214 -9.256 43.733 1.00 44.53 A C ANISOU 846 CB TYR A 117 5018 4782 7119 -701 203 2009 A C ATOM 847 CG TYR A 117 -60.313 -8.331 43.257 1.00 44.60 A C ANISOU 847 CG TYR A 117 5009 4949 6986 -671 307 1805 A C ATOM 848 CD1 TYR A 117 -60.112 -6.956 43.218 1.00 42.66 A C ANISOU 848 CD1 TYR A 117 4721 4810 6680 -592 354 1715 A C ATOM 849 CD2 TYR A 117 -61.551 -8.825 42.864 1.00 44.40 A C ANISOU 849 CD2 TYR A 117 5009 4962 6900 -722 343 1699 A C ATOM 850 CE1 TYR A 117 -61.106 -6.101 42.794 1.00 44.70 A C ANISOU 850 CE1 TYR A 117 4960 5192 6830 -559 421 1526 A C ATOM 851 CE2 TYR A 117 -62.555 -7.975 42.438 1.00 44.43 A C ANISOU 851 CE2 TYR A 117 4986 5096 6800 -688 413 1504 A C ATOM 852 CZ TYR A 117 -62.327 -6.613 42.404 1.00 46.98 A C ANISOU 852 CZ TYR A 117 5266 5509 7075 -604 445 1419 A C ATOM 853 OH TYR A 117 -63.320 -5.759 41.980 1.00 47.16 A O ANISOU 853 OH TYR A 117 5259 5642 7016 -564 489 1222 A O ATOM 854 N PRO A 118 -60.964 -8.969 46.651 1.00 49.22 A N ANISOU 854 N PRO A 118 5622 5816 7263 -1236 131 2058 A N ATOM 855 CA PRO A 118 -61.915 -9.518 47.625 1.00 50.07 A C ANISOU 855 CA PRO A 118 5771 6048 7206 -1500 108 2078 A C ATOM 856 C PRO A 118 -63.192 -10.087 47.026 1.00 52.78 A C ANISOU 856 C PRO A 118 6123 6418 7514 -1533 180 1939 A C ATOM 857 O PRO A 118 -64.002 -10.641 47.777 1.00 54.02 A O ANISOU 857 O PRO A 118 6316 6669 7539 -1765 172 1946 A O ATOM 858 CB PRO A 118 -62.224 -8.302 48.506 1.00 49.07 A C ANISOU 858 CB PRO A 118 5587 6152 6903 -1607 157 1991 A C ATOM 859 CG PRO A 118 -62.105 -7.147 47.571 1.00 47.53 A C ANISOU 859 CG PRO A 118 5315 5976 6767 -1371 243 1832 A C ATOM 860 CD PRO A 118 -60.999 -7.496 46.609 1.00 46.05 A C ANISOU 860 CD PRO A 118 5149 5561 6786 -1154 209 1922 A C ATOM 861 N ALA A 119 -63.404 -9.978 45.718 1.00 55.17 A N ANISOU 861 N ALA A 119 6402 6641 7920 -1327 248 1810 A N ATOM 862 CA ALA A 119 -64.651 -10.405 45.105 1.00 56.11 A C ANISOU 862 CA ALA A 119 6522 6792 8007 -1347 312 1660 A C ATOM 863 C ALA A 119 -64.452 -11.648 44.245 1.00 57.43 A C ANISOU 863 C ALA A 119 6756 6744 8322 -1269 281 1733 A C ATOM 864 O ALA A 119 -63.343 -11.961 43.803 1.00 58.74 A O ANISOU 864 O ALA A 119 6946 6727 8646 -1135 236 1847 A O ATOM 865 CB ALA A 119 -65.256 -9.279 44.259 1.00 57.23 A C ANISOU 865 CB ALA A 119 6592 7018 8134 -1191 403 1432 A C ATOM 866 N ALA A 120 -65.555 -12.355 44.021 1.00 57.78 A N ANISOU 866 N ALA A 120 6821 6812 8322 -1359 310 1653 A N ATOM 867 CA ALA A 120 -65.589 -13.572 43.225 1.00 60.34 A C ANISOU 867 CA ALA A 120 7209 6949 8767 -1309 289 1699 A C ATOM 868 C ALA A 120 -66.967 -13.689 42.596 1.00 60.86 A C ANISOU 868 C ALA A 120 7258 7090 8775 -1325 365 1506 A C ATOM 869 O ALA A 120 -67.940 -13.130 43.116 1.00 64.11 A O ANISOU 869 O ALA A 120 7613 7700 9048 -1445 412 1373 A O ATOM 870 CB ALA A 120 -65.280 -14.812 44.072 1.00 60.91 A C ANISOU 870 CB ALA A 120 7361 6930 8851 -1491 179 1906 A C ATOM 871 N PRO A 121 -67.088 -14.406 41.466 1.00 59.64 A N ANISOU 871 N PRO A 121 7146 6780 8735 -1207 379 1475 A N ATOM 872 CA PRO A 121 -66.000 -15.112 40.786 1.00 58.10 A C ANISOU 872 CA PRO A 121 7006 6347 8721 -1070 341 1599 A C ATOM 873 C PRO A 121 -65.239 -14.212 39.822 1.00 54.75 A C ANISOU 873 C PRO A 121 6560 5856 8387 -839 391 1530 A C ATOM 874 O PRO A 121 -65.849 -13.447 39.076 1.00 54.43 A O ANISOU 874 O PRO A 121 6501 5882 8299 -747 456 1359 A O ATOM 875 CB PRO A 121 -66.732 -16.219 40.029 1.00 58.75 A C ANISOU 875 CB PRO A 121 7141 6329 8852 -1081 356 1554 A C ATOM 876 CG PRO A 121 -68.054 -15.612 39.696 1.00 58.41 A C ANISOU 876 CG PRO A 121 7055 6449 8690 -1097 428 1343 A C ATOM 877 CD PRO A 121 -68.379 -14.609 40.784 1.00 59.35 A C ANISOU 877 CD PRO A 121 7099 6791 8660 -1215 436 1298 A C ATOM 878 N LEU A 122 -63.914 -14.315 39.847 1.00 54.84 A N ANISOU 878 N LEU A 122 6576 5730 8531 -756 353 1660 A N ATOM 879 CA LEU A 122 -63.064 -13.529 38.966 1.00 53.23 A C ANISOU 879 CA LEU A 122 6358 5452 8416 -559 410 1602 A C ATOM 880 C LEU A 122 -62.794 -14.303 37.684 1.00 51.81 A C ANISOU 880 C LEU A 122 6229 5068 8387 -436 454 1565 A C ATOM 881 O LEU A 122 -62.242 -15.408 37.748 1.00 52.75 A O ANISOU 881 O LEU A 122 6366 5026 8649 -452 404 1679 A O ATOM 882 CB LEU A 122 -61.755 -13.190 39.658 1.00 52.46 A C ANISOU 882 CB LEU A 122 6223 5317 8393 -538 357 1739 A C ATOM 883 CG LEU A 122 -61.003 -11.956 39.160 1.00 50.56 A C ANISOU 883 CG LEU A 122 5950 5090 8170 -386 420 1668 A C ATOM 884 CD1 LEU A 122 -61.919 -10.745 39.148 1.00 49.69 A C ANISOU 884 CD1 LEU A 122 5821 5177 7881 -390 469 1519 A C ATOM 885 CD2 LEU A 122 -59.790 -11.692 40.032 1.00 50.44 A C ANISOU 885 CD2 LEU A 122 5888 5054 8224 -394 354 1812 A C ATOM 886 N PRO A 123 -63.166 -13.785 36.518 1.00 51.96 A N ANISOU 886 N PRO A 123 6279 5080 8384 -322 538 1406 A N ATOM 887 CA PRO A 123 -62.869 -14.488 35.269 1.00 50.22 A C ANISOU 887 CA PRO A 123 6118 4667 8295 -220 593 1361 A C ATOM 888 C PRO A 123 -61.421 -14.283 34.850 1.00 53.79 A C ANISOU 888 C PRO A 123 6557 4979 8901 -100 633 1394 A C ATOM 889 O PRO A 123 -60.722 -13.387 35.327 1.00 55.46 A O ANISOU 889 O PRO A 123 6722 5253 9099 -71 627 1427 A O ATOM 890 CB PRO A 123 -63.824 -13.843 34.253 1.00 47.69 A C ANISOU 890 CB PRO A 123 5849 4408 7864 -164 653 1178 A C ATOM 891 CG PRO A 123 -64.670 -12.853 35.039 1.00 48.50 A C ANISOU 891 CG PRO A 123 5898 4731 7799 -233 619 1124 A C ATOM 892 CD PRO A 123 -63.908 -12.539 36.280 1.00 49.03 A C ANISOU 892 CD PRO A 123 5896 4867 7865 -291 575 1256 A C ATOM 893 N GLY A 124 -60.972 -15.147 33.945 1.00 54.17 A N ANISOU 893 N GLY A 124 6642 4836 9105 -36 679 1374 A N ATOM 894 CA GLY A 124 -59.739 -14.871 33.240 1.00 52.74 A C ANISOU 894 CA GLY A 124 6453 4524 9064 81 758 1340 A C ATOM 895 C GLY A 124 -59.865 -13.622 32.393 1.00 49.35 A C ANISOU 895 C GLY A 124 6078 4166 8507 153 849 1198 A C ATOM 896 O GLY A 124 -60.963 -13.162 32.077 1.00 52.59 A O ANISOU 896 O GLY A 124 6545 4683 8754 132 848 1108 A O ATOM 897 N PHE A 125 -58.724 -13.058 32.015 1.00 46.70 A N ANISOU 897 N PHE A 125 5727 3763 8253 233 919 1172 A N ATOM 898 CA PHE A 125 -58.774 -11.862 31.188 1.00 44.87 A C ANISOU 898 CA PHE A 125 5571 3584 7894 286 998 1046 A C ATOM 899 C PHE A 125 -57.475 -11.692 30.420 1.00 46.24 A C ANISOU 899 C PHE A 125 5752 3620 8198 358 1115 992 A C ATOM 900 O PHE A 125 -56.426 -12.226 30.791 1.00 50.30 A O ANISOU 900 O PHE A 125 6174 4032 8908 378 1119 1059 A O ATOM 901 CB PHE A 125 -59.056 -10.592 32.002 1.00 48.97 A C ANISOU 901 CB PHE A 125 6056 4295 8255 270 939 1064 A C ATOM 902 CG PHE A 125 -58.091 -10.354 33.130 1.00 49.88 A C ANISOU 902 CG PHE A 125 6060 4444 8447 262 893 1190 A C ATOM 903 CD1 PHE A 125 -57.995 -11.246 34.184 1.00 51.49 A C ANISOU 903 CD1 PHE A 125 6187 4638 8739 194 800 1331 A C ATOM 904 CD2 PHE A 125 -57.228 -9.271 33.098 1.00 48.48 A C ANISOU 904 CD2 PHE A 125 5866 4293 8259 316 937 1169 A C ATOM 905 CE1 PHE A 125 -57.106 -11.028 35.215 1.00 53.07 A C ANISOU 905 CE1 PHE A 125 6297 4859 9007 179 737 1452 A C ATOM 906 CE2 PHE A 125 -56.327 -9.051 34.121 1.00 48.94 A C ANISOU 906 CE2 PHE A 125 5822 4379 8393 309 888 1283 A C ATOM 907 CZ PHE A 125 -56.265 -9.933 35.181 1.00 50.85 A C ANISOU 907 CZ PHE A 125 5989 4611 8720 241 783 1426 A C ATOM 908 N SER A 126 -57.580 -10.943 29.329 1.00 42.79 A N ANISOU 908 N SER A 126 5430 3176 7652 386 1203 860 A N ATOM 909 CA SER A 126 -56.443 -10.416 28.595 1.00 43.31 A C ANISOU 909 CA SER A 126 5525 3154 7776 429 1329 783 A C ATOM 910 C SER A 126 -56.369 -8.919 28.849 1.00 40.53 A C ANISOU 910 C SER A 126 5196 2938 7267 441 1311 772 A C ATOM 911 O SER A 126 -57.401 -8.254 28.974 1.00 43.59 A O ANISOU 911 O SER A 126 5637 3449 7474 425 1232 754 A O ATOM 912 CB SER A 126 -56.576 -10.680 27.092 1.00 43.11 A C ANISOU 912 CB SER A 126 5648 3008 7725 424 1449 638 A C ATOM 913 OG SER A 126 -56.897 -12.033 26.825 1.00 42.43 A O ANISOU 913 OG SER A 126 5555 2812 7755 408 1455 639 A O ATOM 914 N ALA A 127 -55.151 -8.391 28.932 1.00 39.13 A N ANISOU 914 N ALA A 127 4967 2730 7170 470 1379 773 A N ATOM 915 CA ALA A 127 -54.979 -6.976 29.224 1.00 41.85 A C ANISOU 915 CA ALA A 127 5328 3195 7377 480 1362 769 A C ATOM 916 C ALA A 127 -53.595 -6.539 28.778 1.00 43.86 A C ANISOU 916 C ALA A 127 5572 3367 7725 502 1492 715 A C ATOM 917 O ALA A 127 -52.637 -7.312 28.862 1.00 45.19 A O ANISOU 917 O ALA A 127 5637 3422 8112 519 1550 730 A O ATOM 918 CB ALA A 127 -55.172 -6.683 30.717 1.00 40.76 A C ANISOU 918 CB ALA A 127 5063 3205 7221 471 1230 900 A C ATOM 919 N VAL A 128 -53.502 -5.298 28.307 1.00 42.12 A N ANISOU 919 N VAL A 128 5459 3198 7348 497 1530 645 A N ATOM 920 CA VAL A 128 -52.229 -4.650 28.025 1.00 43.65 A C ANISOU 920 CA VAL A 128 5642 3347 7595 502 1649 595 A C ATOM 921 C VAL A 128 -52.110 -3.422 28.913 1.00 43.59 A C ANISOU 921 C VAL A 128 5591 3486 7487 517 1568 661 A C ATOM 922 O VAL A 128 -53.093 -2.707 29.138 1.00 43.28 A O ANISOU 922 O VAL A 128 5616 3562 7265 513 1463 672 A O ATOM 923 CB VAL A 128 -52.090 -4.256 26.540 1.00 43.87 A C ANISOU 923 CB VAL A 128 5868 3286 7516 457 1789 442 A C ATOM 924 CG1 VAL A 128 -52.463 -5.422 25.643 1.00 43.78 A C ANISOU 924 CG1 VAL A 128 5923 3147 7563 432 1855 371 A C ATOM 925 CG2 VAL A 128 -52.931 -3.026 26.228 1.00 42.94 A C ANISOU 925 CG2 VAL A 128 5918 3261 7135 437 1710 413 A C ATOM 926 N VAL A 129 -50.904 -3.185 29.418 1.00 41.95 A N ANISOU 926 N VAL A 129 5262 3266 7409 535 1614 694 A N ATOM 927 CA VAL A 129 -50.607 -2.036 30.262 1.00 37.99 A C ANISOU 927 CA VAL A 129 4710 2893 6830 546 1553 753 A C ATOM 928 C VAL A 129 -49.738 -1.080 29.461 1.00 37.19 A C ANISOU 928 C VAL A 129 4700 2753 6677 528 1686 648 A C ATOM 929 O VAL A 129 -48.745 -1.494 28.849 1.00 37.12 A O ANISOU 929 O VAL A 129 4668 2621 6814 518 1832 572 A O ATOM 930 CB VAL A 129 -49.905 -2.447 31.568 1.00 39.65 A C ANISOU 930 CB VAL A 129 4715 3129 7220 569 1480 885 A C ATOM 931 CG1 VAL A 129 -49.778 -1.246 32.503 1.00 41.22 A C ANISOU 931 CG1 VAL A 129 4872 3478 7310 570 1404 950 A C ATOM 932 CG2 VAL A 129 -50.649 -3.590 32.237 1.00 38.54 A C ANISOU 932 CG2 VAL A 129 4506 2992 7145 560 1365 984 A C ATOM 933 N VAL A 130 -50.118 0.191 29.455 1.00 34.80 A N ANISOU 933 N VAL A 130 4501 2550 6172 518 1639 634 A N ATOM 934 CA VAL A 130 -49.278 1.260 28.938 1.00 39.24 A C ANISOU 934 CA VAL A 130 5146 3099 6665 490 1739 560 A C ATOM 935 C VAL A 130 -49.201 2.325 30.018 1.00 39.58 A C ANISOU 935 C VAL A 130 5114 3285 6640 515 1636 642 A C ATOM 936 O VAL A 130 -50.138 2.510 30.801 1.00 41.03 A O ANISOU 936 O VAL A 130 5262 3582 6743 536 1490 713 A O ATOM 937 CB VAL A 130 -49.811 1.849 27.614 1.00 35.01 A C ANISOU 937 CB VAL A 130 4866 2511 5923 434 1783 443 A C ATOM 938 CG1 VAL A 130 -49.969 0.751 26.570 1.00 41.38 A C ANISOU 938 CG1 VAL A 130 5754 3183 6786 399 1883 361 A C ATOM 939 CG2 VAL A 130 -51.127 2.574 27.848 1.00 37.09 A C ANISOU 939 CG2 VAL A 130 5221 2879 5993 451 1607 471 A C ATOM 940 N SER A 131 -48.079 3.034 30.057 1.00 40.41 A N ANISOU 940 N SER A 131 5190 3385 6777 503 1721 621 A N ATOM 941 CA SER A 131 -47.826 3.940 31.164 1.00 38.76 A C ANISOU 941 CA SER A 131 4885 3305 6537 526 1633 704 A C ATOM 942 C SER A 131 -46.932 5.081 30.713 1.00 40.23 A C ANISOU 942 C SER A 131 5151 3481 6653 492 1732 634 A C ATOM 943 O SER A 131 -45.999 4.881 29.930 1.00 39.10 A O ANISOU 943 O SER A 131 5033 3230 6594 454 1894 545 A O ATOM 944 CB SER A 131 -47.175 3.196 32.336 1.00 39.20 A C ANISOU 944 CB SER A 131 4710 3378 6807 558 1591 818 A C ATOM 945 OG SER A 131 -46.912 4.078 33.410 1.00 38.34 A O ANISOU 945 OG SER A 131 4516 3393 6658 567 1509 898 A O ATOM 946 N SER A 132 -47.235 6.278 31.211 1.00 40.01 A N ANISOU 946 N SER A 132 5161 3568 6473 497 1638 665 A N ATOM 947 CA SER A 132 -46.356 7.429 31.091 1.00 38.60 A C ANISOU 947 CA SER A 132 5029 3403 6234 467 1704 627 A C ATOM 948 C SER A 132 -45.603 7.712 32.383 1.00 41.37 A C ANISOU 948 C SER A 132 5179 3847 6694 499 1663 724 A C ATOM 949 O SER A 132 -44.886 8.714 32.464 1.00 42.83 A O ANISOU 949 O SER A 132 5380 4062 6832 478 1703 705 A O ATOM 950 CB SER A 132 -47.161 8.666 30.674 1.00 34.23 A C ANISOU 950 CB SER A 132 4677 2895 5436 447 1619 586 A C ATOM 951 OG SER A 132 -48.289 8.854 31.514 1.00 34.29 A O ANISOU 951 OG SER A 132 4633 3017 5378 496 1443 650 A O ATOM 952 N VAL A 133 -45.751 6.857 33.388 1.00 42.32 A N ANISOU 952 N VAL A 133 5122 4008 6948 537 1577 829 A N ATOM 953 CA VAL A 133 -45.032 6.991 34.650 1.00 41.92 A C ANISOU 953 CA VAL A 133 4886 4033 7008 555 1520 934 A C ATOM 954 C VAL A 133 -43.687 6.286 34.500 1.00 40.91 A C ANISOU 954 C VAL A 133 4631 3787 7127 560 1633 915 A C ATOM 955 O VAL A 133 -43.665 5.089 34.171 1.00 44.08 A O ANISOU 955 O VAL A 133 4986 4083 7680 572 1665 903 A O ATOM 956 CB VAL A 133 -45.835 6.405 35.817 1.00 37.44 A C ANISOU 956 CB VAL A 133 4211 3560 6455 568 1362 1058 A C ATOM 957 CG1 VAL A 133 -45.163 6.727 37.142 1.00 35.93 A C ANISOU 957 CG1 VAL A 133 3863 3457 6331 566 1285 1169 A C ATOM 958 CG2 VAL A 133 -47.246 6.955 35.799 1.00 31.17 A C ANISOU 958 CG2 VAL A 133 3531 2865 5449 563 1271 1035 A C ATOM 959 N PRO A 134 -42.565 6.972 34.711 1.00 39.40 A N ANISOU 959 N PRO A 134 4373 3601 6995 551 1693 899 A N ATOM 960 CA PRO A 134 -41.260 6.313 34.566 1.00 41.21 A C ANISOU 960 CA PRO A 134 4457 3711 7490 559 1800 858 A C ATOM 961 C PRO A 134 -41.077 5.249 35.639 1.00 42.38 A C ANISOU 961 C PRO A 134 4407 3840 7856 602 1668 987 A C ATOM 962 O PRO A 134 -41.248 5.515 36.831 1.00 43.72 A O ANISOU 962 O PRO A 134 4503 4118 7993 608 1518 1120 A O ATOM 963 CB PRO A 134 -40.260 7.463 34.731 1.00 41.34 A C ANISOU 963 CB PRO A 134 4448 3771 7489 536 1863 824 A C ATOM 964 CG PRO A 134 -40.995 8.470 35.561 1.00 41.09 A C ANISOU 964 CG PRO A 134 4470 3901 7242 538 1720 920 A C ATOM 965 CD PRO A 134 -42.442 8.366 35.171 1.00 38.89 A C ANISOU 965 CD PRO A 134 4346 3654 6775 537 1657 917 A C ATOM 966 N LEU A 135 -40.738 4.037 35.208 1.00 42.76 A N ANISOU 966 N LEU A 135 4379 3744 8125 622 1720 946 A N ATOM 967 CA LEU A 135 -40.556 2.939 36.147 1.00 45.59 A C ANISOU 967 CA LEU A 135 4565 4052 8705 658 1577 1070 A C ATOM 968 C LEU A 135 -39.319 3.188 36.999 1.00 45.31 A C ANISOU 968 C LEU A 135 4348 4007 8860 676 1527 1122 A C ATOM 969 O LEU A 135 -38.222 3.400 36.473 1.00 45.53 A O ANISOU 969 O LEU A 135 4306 3954 9038 681 1665 1001 A O ATOM 970 CB LEU A 135 -40.417 1.614 35.400 1.00 45.25 A C ANISOU 970 CB LEU A 135 4481 3836 8875 680 1647 994 A C ATOM 971 CG LEU A 135 -41.463 1.305 34.329 1.00 42.52 A C ANISOU 971 CG LEU A 135 4316 3468 8371 658 1730 911 A C ATOM 972 CD1 LEU A 135 -41.550 -0.195 34.078 1.00 44.15 A C ANISOU 972 CD1 LEU A 135 4455 3528 8793 684 1718 904 A C ATOM 973 CD2 LEU A 135 -42.815 1.867 34.722 1.00 36.80 A C ANISOU 973 CD2 LEU A 135 3728 2901 7354 637 1614 999 A C ATOM 974 N GLY A 136 -39.495 3.154 38.318 1.00 43.75 A N ANISOU 974 N GLY A 136 4075 3891 8655 673 1331 1295 A N ATOM 975 CA GLY A 136 -38.390 3.355 39.231 1.00 46.65 A C ANISOU 975 CA GLY A 136 4277 4250 9198 685 1246 1366 A C ATOM 976 C GLY A 136 -37.969 4.793 39.431 1.00 44.96 A C ANISOU 976 C GLY A 136 4088 4158 8836 663 1296 1342 A C ATOM 977 O GLY A 136 -36.912 5.032 40.026 1.00 48.54 A O ANISOU 977 O GLY A 136 4401 4593 9449 673 1255 1371 A O ATOM 978 N GLY A 137 -38.758 5.757 38.965 1.00 42.85 A N ANISOU 978 N GLY A 137 3995 4007 8278 633 1370 1289 A N ATOM 979 CA GLY A 137 -38.423 7.161 39.066 1.00 39.63 A C ANISOU 979 CA GLY A 137 3634 3707 7718 610 1418 1257 A C ATOM 980 C GLY A 137 -38.952 7.872 40.292 1.00 42.78 A C ANISOU 980 C GLY A 137 4037 4274 7941 583 1261 1394 A C ATOM 981 O GLY A 137 -38.773 9.089 40.411 1.00 46.20 A O ANISOU 981 O GLY A 137 4518 4805 8232 564 1291 1369 A O ATOM 982 N GLY A 138 -39.576 7.151 41.221 1.00 43.23 A N ANISOU 982 N GLY A 138 4052 4370 8004 570 1097 1532 A N ATOM 983 CA GLY A 138 -40.080 7.748 42.437 1.00 44.06 A C ANISOU 983 CA GLY A 138 4158 4638 7945 521 956 1652 A C ATOM 984 C GLY A 138 -41.459 8.358 42.341 1.00 43.93 A C ANISOU 984 C GLY A 138 4287 4756 7649 494 952 1622 A C ATOM 985 O GLY A 138 -41.933 8.933 43.328 1.00 46.98 A O ANISOU 985 O GLY A 138 4673 5289 7890 445 854 1693 A O ATOM 986 N LEU A 139 -42.117 8.260 41.191 1.00 41.45 A N ANISOU 986 N LEU A 139 4094 4394 7261 519 1052 1509 A N ATOM 987 CA LEU A 139 -43.473 8.761 41.038 1.00 39.11 A C ANISOU 987 CA LEU A 139 3925 4202 6730 502 1029 1467 A C ATOM 988 C LEU A 139 -44.515 7.678 41.287 1.00 40.86 A C ANISOU 988 C LEU A 139 4150 4429 6947 481 949 1520 A C ATOM 989 O LEU A 139 -45.683 7.856 40.924 1.00 35.78 A O ANISOU 989 O LEU A 139 3606 3839 6149 476 945 1459 A O ATOM 990 CB LEU A 139 -43.639 9.382 39.650 1.00 38.33 A C ANISOU 990 CB LEU A 139 3980 4048 6536 530 1159 1317 A C ATOM 991 CG LEU A 139 -42.558 10.443 39.413 1.00 40.88 A C ANISOU 991 CG LEU A 139 4309 4364 6859 531 1245 1265 A C ATOM 992 CD1 LEU A 139 -42.676 11.088 38.041 1.00 43.22 A C ANISOU 992 CD1 LEU A 139 4785 4596 7039 531 1367 1123 A C ATOM 993 CD2 LEU A 139 -42.591 11.487 40.522 1.00 40.84 A C ANISOU 993 CD2 LEU A 139 4264 4513 6742 508 1152 1328 A C ATOM 994 N SER A 140 -44.110 6.565 41.902 1.00 40.80 A N ANISOU 994 N SER A 140 4033 4358 7110 465 875 1631 A N ATOM 995 CA SER A 140 -45.002 5.469 42.283 1.00 38.89 A C ANISOU 995 CA SER A 140 3790 4117 6870 426 786 1702 A C ATOM 996 C SER A 140 -45.695 4.865 41.060 1.00 37.95 A C ANISOU 996 C SER A 140 3765 3906 6746 464 871 1599 A C ATOM 997 O SER A 140 -46.922 4.820 40.959 1.00 41.11 A O ANISOU 997 O SER A 140 4242 4376 7001 440 848 1567 A O ATOM 998 CB SER A 140 -46.017 5.929 43.337 1.00 39.45 A C ANISOU 998 CB SER A 140 3876 4373 6740 344 686 1754 A C ATOM 999 OG SER A 140 -46.698 7.107 42.941 1.00 44.30 A O ANISOU 999 OG SER A 140 4576 5090 7165 360 740 1638 A O ATOM 1000 N SER A 141 -44.871 4.389 40.123 1.00 38.85 A N ANISOU 1000 N SER A 141 3869 3861 7033 517 973 1536 A N ATOM 1001 CA SER A 141 -45.386 3.550 39.047 1.00 40.07 A C ANISOU 1001 CA SER A 141 4099 3904 7223 542 1044 1457 A C ATOM 1002 C SER A 141 -45.954 2.239 39.581 1.00 44.73 A C ANISOU 1002 C SER A 141 4644 4462 7891 512 937 1557 A C ATOM 1003 O SER A 141 -46.935 1.721 39.035 1.00 48.73 A O ANISOU 1003 O SER A 141 5232 4954 8329 507 951 1513 A O ATOM 1004 CB SER A 141 -44.284 3.275 38.023 1.00 41.73 A C ANISOU 1004 CB SER A 141 4288 3949 7616 587 1187 1359 A C ATOM 1005 OG SER A 141 -43.211 2.552 38.605 1.00 45.53 A O ANISOU 1005 OG SER A 141 4608 4335 8355 603 1139 1434 A O ATOM 1006 N SER A 142 -45.353 1.687 40.639 1.00 45.33 A N ANISOU 1006 N SER A 142 4599 4518 8106 485 819 1694 A N ATOM 1007 CA SER A 142 -45.865 0.453 41.228 1.00 42.91 A C ANISOU 1007 CA SER A 142 4267 4175 7863 438 698 1805 A C ATOM 1008 C SER A 142 -47.313 0.619 41.671 1.00 44.84 A C ANISOU 1008 C SER A 142 4593 4577 7867 362 644 1822 A C ATOM 1009 O SER A 142 -48.186 -0.176 41.300 1.00 48.15 A O ANISOU 1009 O SER A 142 5065 4966 8264 346 643 1803 A O ATOM 1010 CB SER A 142 -44.983 0.030 42.402 1.00 41.80 A C ANISOU 1010 CB SER A 142 4006 3996 7881 403 548 1962 A C ATOM 1011 OG SER A 142 -45.076 0.965 43.463 1.00 45.66 A O ANISOU 1011 OG SER A 142 4489 4654 8207 335 474 2035 A O ATOM 1012 N ALA A 143 -47.586 1.651 42.472 1.00 42.61 A N ANISOU 1012 N ALA A 143 4312 4465 7411 311 604 1844 A N ATOM 1013 CA ALA A 143 -48.950 1.890 42.928 1.00 44.17 A C ANISOU 1013 CA ALA A 143 4566 4822 7395 234 565 1830 A C ATOM 1014 C ALA A 143 -49.871 2.195 41.755 1.00 41.91 A C ANISOU 1014 C ALA A 143 4379 4538 7006 288 662 1673 A C ATOM 1015 O ALA A 143 -51.023 1.747 41.726 1.00 43.35 A O ANISOU 1015 O ALA A 143 4602 4766 7102 246 640 1646 A O ATOM 1016 CB ALA A 143 -48.971 3.034 43.941 1.00 44.23 A C ANISOU 1016 CB ALA A 143 4546 5004 7254 174 520 1856 A C ATOM 1017 N SER A 144 -49.377 2.952 40.772 1.00 40.41 A N ANISOU 1017 N SER A 144 4238 4296 6822 372 765 1567 A N ATOM 1018 CA SER A 144 -50.156 3.201 39.563 1.00 41.11 A C ANISOU 1018 CA SER A 144 4444 4356 6820 418 841 1426 A C ATOM 1019 C SER A 144 -50.582 1.893 38.907 1.00 40.01 A C ANISOU 1019 C SER A 144 4336 4097 6769 424 859 1417 A C ATOM 1020 O SER A 144 -51.741 1.731 38.507 1.00 38.95 A O ANISOU 1020 O SER A 144 4272 3993 6534 413 849 1351 A O ATOM 1021 CB SER A 144 -49.350 4.057 38.585 1.00 40.00 A C ANISOU 1021 CB SER A 144 4367 4144 6686 483 949 1332 A C ATOM 1022 OG SER A 144 -50.139 4.427 37.468 1.00 41.83 A O ANISOU 1022 OG SER A 144 4739 4352 6801 510 996 1204 A O ATOM 1023 N LEU A 145 -49.647 0.949 38.777 1.00 33.23 A N ANISOU 1023 N LEU A 145 3418 3094 6112 444 880 1473 A N ATOM 1024 CA LEU A 145 -49.972 -0.341 38.177 1.00 33.86 A C ANISOU 1024 CA LEU A 145 3521 3049 6297 450 896 1465 A C ATOM 1025 C LEU A 145 -50.985 -1.103 39.020 1.00 43.21 A C ANISOU 1025 C LEU A 145 4686 4304 7426 371 782 1552 A C ATOM 1026 O LEU A 145 -51.925 -1.703 38.486 1.00 46.18 A O ANISOU 1026 O LEU A 145 5127 4659 7762 362 793 1502 A O ATOM 1027 CB LEU A 145 -48.698 -1.166 37.992 1.00 34.98 A C ANISOU 1027 CB LEU A 145 3578 3017 6697 489 928 1501 A C ATOM 1028 CG LEU A 145 -48.839 -2.579 37.417 1.00 43.92 A C ANISOU 1028 CG LEU A 145 4714 3994 7982 500 942 1494 A C ATOM 1029 CD1 LEU A 145 -49.603 -2.544 36.107 1.00 35.42 A C ANISOU 1029 CD1 LEU A 145 3771 2886 6800 522 1052 1350 A C ATOM 1030 CD2 LEU A 145 -47.473 -3.218 37.212 1.00 37.11 A C ANISOU 1030 CD2 LEU A 145 3745 2954 7401 549 978 1497 A C ATOM 1031 N GLU A 146 -50.799 -1.104 40.341 1.00 42.88 A N ANISOU 1031 N GLU A 146 4565 4348 7378 300 673 1681 A N ATOM 1032 CA GLU A 146 -51.686 -1.863 41.214 1.00 40.59 A C ANISOU 1032 CA GLU A 146 4269 4126 7029 193 569 1769 A C ATOM 1033 C GLU A 146 -53.099 -1.294 41.197 1.00 39.14 A C ANISOU 1033 C GLU A 146 4141 4099 6629 149 582 1671 A C ATOM 1034 O GLU A 146 -54.078 -2.038 41.066 1.00 40.65 A O ANISOU 1034 O GLU A 146 4366 4294 6783 103 566 1651 A O ATOM 1035 CB GLU A 146 -51.135 -1.866 42.639 1.00 44.59 A C ANISOU 1035 CB GLU A 146 4699 4692 7550 103 449 1926 A C ATOM 1036 CG GLU A 146 -49.687 -2.304 42.762 1.00 47.59 A C ANISOU 1036 CG GLU A 146 5003 4916 8163 152 408 2018 A C ATOM 1037 CD GLU A 146 -49.069 -1.818 44.052 1.00 48.64 A C ANISOU 1037 CD GLU A 146 5074 5132 8273 79 299 2144 A C ATOM 1038 OE1 GLU A 146 -49.728 -1.013 44.741 1.00 46.63 A O ANISOU 1038 OE1 GLU A 146 4842 5064 7812 -2 285 2138 A O ATOM 1039 OE2 GLU A 146 -47.944 -2.245 44.391 1.00 52.75 A O1- ANISOU 1039 OE2 GLU A 146 5523 5530 8991 99 222 2242 A O1- ATOM 1040 N VAL A 147 -53.223 0.029 41.313 1.00 40.35 A N ANISOU 1040 N VAL A 147 4300 4378 6653 165 606 1598 A N ATOM 1041 CA VAL A 147 -54.544 0.646 41.377 1.00 42.13 A C ANISOU 1041 CA VAL A 147 4555 4750 6701 128 602 1489 A C ATOM 1042 C VAL A 147 -55.258 0.523 40.036 1.00 38.68 A C ANISOU 1042 C VAL A 147 4208 4237 6252 203 659 1355 A C ATOM 1043 O VAL A 147 -56.472 0.292 39.984 1.00 32.17 A O ANISOU 1043 O VAL A 147 3401 3473 5348 163 638 1285 A O ATOM 1044 CB VAL A 147 -54.423 2.112 41.831 1.00 36.06 A C ANISOU 1044 CB VAL A 147 3764 4116 5822 135 601 1440 A C ATOM 1045 CG1 VAL A 147 -55.773 2.792 41.785 1.00 34.13 A C ANISOU 1045 CG1 VAL A 147 3536 4002 5430 115 593 1298 A C ATOM 1046 CG2 VAL A 147 -53.830 2.179 43.232 1.00 32.29 A C ANISOU 1046 CG2 VAL A 147 3205 3727 5338 38 536 1575 A C ATOM 1047 N ALA A 148 -54.522 0.668 38.932 1.00 36.85 A N ANISOU 1047 N ALA A 148 4037 3869 6096 301 734 1310 A N ATOM 1048 CA ALA A 148 -55.110 0.403 37.623 1.00 34.08 A C ANISOU 1048 CA ALA A 148 3792 3423 5736 355 784 1197 A C ATOM 1049 C ALA A 148 -55.644 -1.022 37.556 1.00 40.08 A C ANISOU 1049 C ALA A 148 4547 4116 6565 314 767 1236 A C ATOM 1050 O ALA A 148 -56.775 -1.256 37.116 1.00 39.41 A O ANISOU 1050 O ALA A 148 4512 4049 6411 303 754 1154 A O ATOM 1051 CB ALA A 148 -54.082 0.651 36.519 1.00 31.93 A C ANISOU 1051 CB ALA A 148 3589 3006 5535 433 883 1152 A C ATOM 1052 N THR A 149 -54.830 -1.991 37.981 1.00 35.64 A N ANISOU 1052 N THR A 149 3923 3466 6151 293 757 1358 A N ATOM 1053 CA THR A 149 -55.281 -3.377 38.038 1.00 37.98 A C ANISOU 1053 CA THR A 149 4215 3694 6523 245 724 1411 A C ATOM 1054 C THR A 149 -56.542 -3.516 38.880 1.00 40.44 A C ANISOU 1054 C THR A 149 4508 4156 6701 137 650 1420 A C ATOM 1055 O THR A 149 -57.524 -4.132 38.449 1.00 40.37 A O ANISOU 1055 O THR A 149 4541 4135 6661 115 651 1363 A O ATOM 1056 CB THR A 149 -54.171 -4.265 38.599 1.00 38.75 A C ANISOU 1056 CB THR A 149 4237 3678 6807 231 685 1554 A C ATOM 1057 CG2 THR A 149 -54.660 -5.702 38.741 1.00 35.92 A C ANISOU 1057 CG2 THR A 149 3882 3243 6523 171 630 1621 A C ATOM 1058 OG1 THR A 149 -53.036 -4.228 37.725 1.00 42.20 A O ANISOU 1058 OG1 THR A 149 4675 3966 7393 328 774 1513 A O ATOM 1059 N TYR A 150 -56.533 -2.956 40.094 1.00 34.03 A N ANISOU 1059 N TYR A 150 3631 3489 5808 59 591 1482 A N ATOM 1060 CA TYR A 150 -57.694 -3.098 40.967 1.00 38.18 A C ANISOU 1060 CA TYR A 150 4132 4168 6206 -71 538 1476 A C ATOM 1061 C TYR A 150 -58.950 -2.554 40.301 1.00 39.85 A C ANISOU 1061 C TYR A 150 4378 4454 6308 -43 569 1298 A C ATOM 1062 O TYR A 150 -59.999 -3.207 40.301 1.00 39.98 A O ANISOU 1062 O TYR A 150 4401 4502 6288 -110 556 1254 A O ATOM 1063 CB TYR A 150 -57.459 -2.403 42.309 1.00 40.15 A C ANISOU 1063 CB TYR A 150 4315 4570 6369 -168 488 1544 A C ATOM 1064 CG TYR A 150 -58.471 -2.821 43.355 1.00 42.71 A C ANISOU 1064 CG TYR A 150 4614 5035 6577 -344 441 1562 A C ATOM 1065 CD1 TYR A 150 -59.777 -2.349 43.311 1.00 34.72 A C ANISOU 1065 CD1 TYR A 150 3590 4161 5442 -384 469 1402 A C ATOM 1066 CD2 TYR A 150 -58.127 -3.697 44.375 1.00 45.81 A C ANISOU 1066 CD2 TYR A 150 4999 5416 6988 -483 363 1730 A C ATOM 1067 CE1 TYR A 150 -60.711 -2.735 44.251 1.00 36.32 A C ANISOU 1067 CE1 TYR A 150 3762 4498 5539 -563 448 1395 A C ATOM 1068 CE2 TYR A 150 -59.055 -4.086 45.326 1.00 45.38 A C ANISOU 1068 CE2 TYR A 150 4941 5493 6807 -674 331 1742 A C ATOM 1069 CZ TYR A 150 -60.345 -3.602 45.259 1.00 43.34 A C ANISOU 1069 CZ TYR A 150 4660 5383 6423 -718 386 1566 A C ATOM 1070 OH TYR A 150 -61.274 -3.986 46.200 1.00 47.43 A O ANISOU 1070 OH TYR A 150 5168 6039 6816 -926 375 1555 A O ATOM 1071 N THR A 151 -58.862 -1.352 39.728 1.00 38.00 A N ANISOU 1071 N THR A 151 4168 4242 6028 52 600 1191 A N ATOM 1072 CA THR A 151 -60.018 -0.787 39.043 1.00 37.57 A C ANISOU 1072 CA THR A 151 4151 4233 5889 90 599 1020 A C ATOM 1073 C THR A 151 -60.441 -1.664 37.874 1.00 39.40 A C ANISOU 1073 C THR A 151 4468 4327 6176 136 622 972 A C ATOM 1074 O THR A 151 -61.635 -1.754 37.566 1.00 36.55 A O ANISOU 1074 O THR A 151 4118 4004 5764 121 598 860 A O ATOM 1075 CB THR A 151 -59.712 0.628 38.550 1.00 34.68 A C ANISOU 1075 CB THR A 151 3822 3878 5476 187 607 931 A C ATOM 1076 CG2 THR A 151 -61.003 1.350 38.174 1.00 36.00 A C ANISOU 1076 CG2 THR A 151 4002 4117 5560 208 563 755 A C ATOM 1077 OG1 THR A 151 -59.037 1.364 39.578 1.00 33.77 A O ANISOU 1077 OG1 THR A 151 3634 3865 5333 152 597 997 A O ATOM 1078 N PHE A 152 -59.480 -2.309 37.208 1.00 41.50 A N ANISOU 1078 N PHE A 152 4786 4429 6553 191 671 1043 A N ATOM 1079 CA PHE A 152 -59.824 -3.209 36.112 1.00 41.15 A C ANISOU 1079 CA PHE A 152 4824 4248 6564 224 703 999 A C ATOM 1080 C PHE A 152 -60.639 -4.390 36.621 1.00 42.66 A C ANISOU 1080 C PHE A 152 4977 4465 6769 127 666 1040 A C ATOM 1081 O PHE A 152 -61.697 -4.714 36.072 1.00 44.94 A O ANISOU 1081 O PHE A 152 5304 4751 7019 120 657 945 A O ATOM 1082 CB PHE A 152 -58.560 -3.711 35.416 1.00 40.25 A C ANISOU 1082 CB PHE A 152 4752 3958 6585 286 776 1056 A C ATOM 1083 CG PHE A 152 -58.833 -4.484 34.157 1.00 43.30 A C ANISOU 1083 CG PHE A 152 5237 4197 7016 321 827 988 A C ATOM 1084 CD1 PHE A 152 -59.648 -3.951 33.171 1.00 43.36 A C ANISOU 1084 CD1 PHE A 152 5352 4199 6924 356 826 852 A C ATOM 1085 CD2 PHE A 152 -58.324 -5.760 33.979 1.00 43.72 A C ANISOU 1085 CD2 PHE A 152 5280 4116 7218 314 860 1057 A C ATOM 1086 CE1 PHE A 152 -59.914 -4.654 32.014 1.00 39.04 A C ANISOU 1086 CE1 PHE A 152 4909 3520 6405 375 869 790 A C ATOM 1087 CE2 PHE A 152 -58.595 -6.471 32.823 1.00 43.06 A C ANISOU 1087 CE2 PHE A 152 5288 3900 7172 338 914 984 A C ATOM 1088 CZ PHE A 152 -59.391 -5.916 31.841 1.00 39.77 A C ANISOU 1088 CZ PHE A 152 4986 3487 6636 364 923 853 A C ATOM 1089 N LEU A 153 -60.152 -5.052 37.675 1.00 44.78 A N ANISOU 1089 N LEU A 153 5176 4750 7089 45 636 1184 A N ATOM 1090 CA LEU A 153 -60.868 -6.196 38.230 1.00 40.18 A C ANISOU 1090 CA LEU A 153 4572 4186 6509 -71 596 1239 A C ATOM 1091 C LEU A 153 -62.263 -5.810 38.700 1.00 39.38 A C ANISOU 1091 C LEU A 153 4435 4260 6266 -159 570 1130 A C ATOM 1092 O LEU A 153 -63.176 -6.644 38.689 1.00 41.52 A O ANISOU 1092 O LEU A 153 4713 4540 6522 -234 559 1103 A O ATOM 1093 CB LEU A 153 -60.067 -6.804 39.380 1.00 39.23 A C ANISOU 1093 CB LEU A 153 4400 4056 6450 -161 541 1421 A C ATOM 1094 CG LEU A 153 -58.649 -7.236 39.011 1.00 40.66 A C ANISOU 1094 CG LEU A 153 4585 4054 6810 -74 552 1518 A C ATOM 1095 CD1 LEU A 153 -57.984 -7.928 40.186 1.00 42.94 A C ANISOU 1095 CD1 LEU A 153 4825 4318 7171 -172 458 1702 A C ATOM 1096 CD2 LEU A 153 -58.674 -8.142 37.790 1.00 38.48 A C ANISOU 1096 CD2 LEU A 153 4371 3603 6647 -1 605 1469 A C ATOM 1097 N GLN A 154 -62.447 -4.555 39.116 1.00 36.51 A N ANISOU 1097 N GLN A 154 4027 4037 5809 -153 563 1054 A N ATOM 1098 CA GLN A 154 -63.778 -4.091 39.487 1.00 38.93 A C ANISOU 1098 CA GLN A 154 4279 4504 6008 -225 546 912 A C ATOM 1099 C GLN A 154 -64.725 -4.163 38.302 1.00 42.36 A C ANISOU 1099 C GLN A 154 4766 4879 6450 -149 546 760 A C ATOM 1100 O GLN A 154 -65.935 -4.348 38.478 1.00 41.17 A O ANISOU 1100 O GLN A 154 4571 4818 6254 -221 530 650 A O ATOM 1101 CB GLN A 154 -63.704 -2.661 40.025 1.00 37.75 A C ANISOU 1101 CB GLN A 154 4070 4490 5783 -209 536 843 A C ATOM 1102 CG GLN A 154 -63.112 -2.557 41.424 1.00 39.54 A C ANISOU 1102 CG GLN A 154 4231 4825 5967 -330 526 968 A C ATOM 1103 CD GLN A 154 -62.990 -1.124 41.904 1.00 41.41 A C ANISOU 1103 CD GLN A 154 4412 5188 6134 -309 523 894 A C ATOM 1104 NE2 GLN A 154 -64.073 -0.597 42.462 1.00 40.16 A N ANISOU 1104 NE2 GLN A 154 4174 5193 5892 -392 521 748 A N ATOM 1105 OE1 GLN A 154 -61.935 -0.499 41.779 1.00 44.23 A O ANISOU 1105 OE1 GLN A 154 4789 5496 6520 -224 527 957 A O ATOM 1106 N GLN A 155 -64.193 -4.010 37.089 1.00 43.23 A N ANISOU 1106 N GLN A 155 4973 4839 6614 -14 565 744 A N ATOM 1107 CA GLN A 155 -65.016 -4.152 35.895 1.00 40.43 A C ANISOU 1107 CA GLN A 155 4694 4404 6262 50 554 616 A C ATOM 1108 C GLN A 155 -65.374 -5.612 35.645 1.00 43.78 A C ANISOU 1108 C GLN A 155 5146 4748 6742 -6 570 660 A C ATOM 1109 O GLN A 155 -66.506 -5.920 35.258 1.00 45.13 A O ANISOU 1109 O GLN A 155 5322 4934 6892 -27 545 551 A O ATOM 1110 CB GLN A 155 -64.291 -3.553 34.693 1.00 36.35 A C ANISOU 1110 CB GLN A 155 4297 3750 5764 180 574 590 A C ATOM 1111 CG GLN A 155 -63.673 -2.197 34.987 1.00 35.57 A C ANISOU 1111 CG GLN A 155 4182 3712 5620 229 564 580 A C ATOM 1112 CD GLN A 155 -64.670 -1.225 35.586 1.00 39.63 A C ANISOU 1112 CD GLN A 155 4611 4386 6060 206 494 455 A C ATOM 1113 NE2 GLN A 155 -64.412 -0.791 36.814 1.00 37.73 A N ANISOU 1113 NE2 GLN A 155 4262 4284 5790 142 497 502 A N ATOM 1114 OE1 GLN A 155 -65.665 -0.876 34.956 1.00 42.82 A O ANISOU 1114 OE1 GLN A 155 5044 4785 6441 243 432 310 A O ATOM 1115 N LEU A 156 -64.420 -6.525 35.856 1.00 46.52 A N ANISOU 1115 N LEU A 156 5506 4999 7171 -28 604 816 A N ATOM 1116 CA LEU A 156 -64.717 -7.947 35.707 1.00 47.37 A C ANISOU 1116 CA LEU A 156 5637 5021 7339 -87 610 868 A C ATOM 1117 C LEU A 156 -65.638 -8.434 36.818 1.00 48.72 A C ANISOU 1117 C LEU A 156 5729 5333 7448 -246 575 880 A C ATOM 1118 O LEU A 156 -66.501 -9.291 36.589 1.00 51.66 A O ANISOU 1118 O LEU A 156 6117 5689 7822 -304 570 841 A O ATOM 1119 CB LEU A 156 -63.422 -8.761 35.702 1.00 48.21 A C ANISOU 1119 CB LEU A 156 5766 4977 7576 -67 637 1024 A C ATOM 1120 CG LEU A 156 -62.292 -8.352 34.758 1.00 47.69 A C ANISOU 1120 CG LEU A 156 5760 4773 7588 63 697 1018 A C ATOM 1121 CD1 LEU A 156 -61.063 -9.202 35.028 1.00 49.32 A C ANISOU 1121 CD1 LEU A 156 5941 4847 7950 66 710 1162 A C ATOM 1122 CD2 LEU A 156 -62.726 -8.493 33.310 1.00 48.00 A C ANISOU 1122 CD2 LEU A 156 5910 4702 7626 134 739 895 A C ATOM 1123 N CYS A 157 -65.471 -7.896 38.025 1.00 51.99 A N ANISOU 1123 N CYS A 157 6066 5889 7800 -331 555 929 A N ATOM 1124 CA CYS A 157 -66.191 -8.353 39.205 1.00 53.20 A C ANISOU 1124 CA CYS A 157 6155 6181 7877 -518 535 953 A C ATOM 1125 C CYS A 157 -66.212 -7.236 40.243 1.00 56.70 A C ANISOU 1125 C CYS A 157 6514 6807 8222 -581 529 920 A C ATOM 1126 O CYS A 157 -65.292 -7.132 41.064 1.00 58.88 A O ANISOU 1126 O CYS A 157 6779 7098 8494 -628 512 1061 A O ATOM 1127 CB CYS A 157 -65.549 -9.617 39.778 1.00 52.20 A C ANISOU 1127 CB CYS A 157 6062 5962 7810 -616 507 1150 A C ATOM 1128 SG CYS A 157 -66.450 -10.356 41.160 1.00 56.98 A S ANISOU 1128 SG CYS A 157 6634 6716 8300 -886 479 1193 A S ATOM 1129 N PRO A 158 -67.243 -6.392 40.243 1.00 58.25 A N ANISOU 1129 N PRO A 158 6645 7138 8348 -587 536 730 A N ATOM 1130 CA PRO A 158 -67.244 -5.227 41.137 1.00 57.79 A C ANISOU 1130 CA PRO A 158 6502 7248 8210 -631 538 674 A C ATOM 1131 C PRO A 158 -67.148 -5.644 42.598 1.00 61.64 A C ANISOU 1131 C PRO A 158 6950 7855 8616 -846 542 784 A C ATOM 1132 O PRO A 158 -67.714 -6.658 43.013 1.00 58.56 A O ANISOU 1132 O PRO A 158 6568 7486 8194 -1001 546 815 A O ATOM 1133 CB PRO A 158 -68.583 -4.545 40.832 1.00 56.90 A C ANISOU 1133 CB PRO A 158 6314 7238 8069 -615 537 427 A C ATOM 1134 CG PRO A 158 -69.428 -5.610 40.203 1.00 56.66 A C ANISOU 1134 CG PRO A 158 6315 7140 8073 -641 537 380 A C ATOM 1135 CD PRO A 158 -68.482 -6.494 39.455 1.00 57.10 A C ANISOU 1135 CD PRO A 158 6493 6996 8208 -557 535 550 A C ATOM 1136 N ASP A 159 -66.418 -4.850 43.377 1.00 63.51 A N ANISOU 1136 N ASP A 159 7156 8168 8809 -867 536 845 A N ATOM 1137 CA ASP A 159 -66.235 -5.123 44.793 1.00 67.41 A C ANISOU 1137 CA ASP A 159 7631 8775 9207 -1082 529 957 A C ATOM 1138 C ASP A 159 -67.278 -4.373 45.619 1.00 76.48 A C ANISOU 1138 C ASP A 159 8674 10150 10236 -1226 575 772 A C ATOM 1139 O ASP A 159 -68.018 -3.525 45.118 1.00 74.60 A O ANISOU 1139 O ASP A 159 8362 9971 10012 -1132 599 560 A O ATOM 1140 CB ASP A 159 -64.820 -4.746 45.242 1.00 62.52 A C ANISOU 1140 CB ASP A 159 7038 8109 8610 -1042 491 1134 A C ATOM 1141 CG ASP A 159 -64.593 -3.242 45.290 1.00 58.55 A C ANISOU 1141 CG ASP A 159 6472 7698 8077 -946 511 1029 A C ATOM 1142 OD1 ASP A 159 -65.481 -2.471 44.870 1.00 58.05 A O ANISOU 1142 OD1 ASP A 159 6349 7712 7995 -886 542 821 A O ATOM 1143 OD2 ASP A 159 -63.515 -2.827 45.760 1.00 59.18 A O1- ANISOU 1143 OD2 ASP A 159 6559 7765 8160 -930 485 1155 A O1- ATOM 1144 N SER A 160 -67.332 -4.702 46.905 1.00 89.95 A N ANISOU 1144 N SER A 160 10376 11975 11826 -1467 583 846 A N ATOM 1145 CA SER A 160 -68.309 -4.121 47.816 1.00 92.50 A C ANISOU 1145 CA SER A 160 10597 12522 12026 -1651 648 665 A C ATOM 1146 C SER A 160 -67.721 -3.047 48.719 1.00 92.43 A C ANISOU 1146 C SER A 160 10546 12633 11940 -1697 655 678 A C ATOM 1147 O SER A 160 -68.376 -2.033 48.978 1.00 96.93 A O ANISOU 1147 O SER A 160 11003 13353 12474 -1712 709 465 A O ATOM 1148 CB SER A 160 -68.941 -5.221 48.674 1.00 95.72 A C ANISOU 1148 CB SER A 160 11039 13004 12324 -1938 672 707 A C ATOM 1149 OG SER A 160 -69.602 -4.680 49.804 1.00 98.97 A O ANISOU 1149 OG SER A 160 11370 13640 12594 -2166 745 569 A O ATOM 1150 N GLY A 161 -66.498 -3.248 49.200 1.00 88.50 A N ANISOU 1150 N GLY A 161 10129 12065 11432 -1718 595 915 A N ATOM 1151 CA GLY A 161 -65.933 -2.428 50.253 1.00 82.60 A C ANISOU 1151 CA GLY A 161 9358 11437 10588 -1818 594 958 A C ATOM 1152 C GLY A 161 -65.672 -0.977 49.905 1.00 77.38 A C ANISOU 1152 C GLY A 161 8616 10815 9968 -1631 614 831 A C ATOM 1153 O GLY A 161 -66.195 -0.449 48.918 1.00 78.37 A O ANISOU 1153 O GLY A 161 8688 10909 10178 -1448 633 658 A O ATOM 1154 N THR A 162 -64.860 -0.328 50.733 1.00 71.73 A N ANISOU 1154 N THR A 162 7901 10163 9189 -1686 596 922 A N ATOM 1155 CA THR A 162 -64.597 1.099 50.660 1.00 64.12 A C ANISOU 1155 CA THR A 162 6863 9261 8238 -1556 615 808 A C ATOM 1156 C THR A 162 -63.369 1.365 49.792 1.00 54.53 A C ANISOU 1156 C THR A 162 5704 7867 7147 -1310 556 943 A C ATOM 1157 O THR A 162 -62.606 0.459 49.454 1.00 53.50 A O ANISOU 1157 O THR A 162 5659 7578 7092 -1265 503 1134 A O ATOM 1158 CB THR A 162 -64.387 1.670 52.065 1.00 67.26 A C ANISOU 1158 CB THR A 162 7233 9834 8490 -1766 636 825 A C ATOM 1159 CG2 THR A 162 -64.515 3.186 52.055 1.00 70.09 A C ANISOU 1159 CG2 THR A 162 7487 10294 8851 -1664 676 634 A C ATOM 1160 OG1 THR A 162 -65.365 1.120 52.958 1.00 68.55 A O ANISOU 1160 OG1 THR A 162 7380 10147 8521 -2049 695 747 A O ATOM 1161 N ILE A 163 -63.188 2.633 49.416 1.00 51.25 A N ANISOU 1161 N ILE A 163 5238 7473 6762 -1155 568 828 A N ATOM 1162 CA ILE A 163 -61.985 3.007 48.676 1.00 50.75 A C ANISOU 1162 CA ILE A 163 5228 7258 6798 -950 529 942 A C ATOM 1163 C ILE A 163 -60.739 2.714 49.501 1.00 47.10 A C ANISOU 1163 C ILE A 163 4809 6767 6319 -1032 481 1177 A C ATOM 1164 O ILE A 163 -59.707 2.295 48.964 1.00 46.98 A O ANISOU 1164 O ILE A 163 4851 6586 6412 -916 440 1329 A O ATOM 1165 CB ILE A 163 -62.045 4.483 48.238 1.00 52.89 A C ANISOU 1165 CB ILE A 163 5448 7566 7082 -800 543 777 A C ATOM 1166 CG1 ILE A 163 -63.274 4.735 47.358 1.00 54.69 A C ANISOU 1166 CG1 ILE A 163 5638 7791 7350 -708 555 549 A C ATOM 1167 CG2 ILE A 163 -60.753 4.883 47.540 1.00 51.95 A C ANISOU 1167 CG2 ILE A 163 5393 7299 7046 -619 515 895 A C ATOM 1168 CD1 ILE A 163 -63.352 6.143 46.795 1.00 55.09 A C ANISOU 1168 CD1 ILE A 163 5660 7841 7432 -547 536 391 A C ATOM 1169 N ALA A 164 -60.807 2.938 50.816 1.00 45.82 A N ANISOU 1169 N ALA A 164 4619 6764 6028 -1239 483 1201 A N ATOM 1170 CA ALA A 164 -59.666 2.624 51.671 1.00 46.92 A C ANISOU 1170 CA ALA A 164 4808 6873 6146 -1336 412 1431 A C ATOM 1171 C ALA A 164 -59.335 1.138 51.620 1.00 46.90 A C ANISOU 1171 C ALA A 164 4890 6725 6207 -1393 340 1624 A C ATOM 1172 O ALA A 164 -58.159 0.755 51.605 1.00 49.88 A O ANISOU 1172 O ALA A 164 5309 6961 6680 -1335 259 1814 A O ATOM 1173 CB ALA A 164 -59.944 3.060 53.109 1.00 46.91 A C ANISOU 1173 CB ALA A 164 4780 7074 5969 -1585 427 1412 A C ATOM 1174 N ALA A 165 -60.361 0.284 51.583 1.00 44.76 A N ANISOU 1174 N ALA A 165 4635 6475 5894 -1504 364 1569 A N ATOM 1175 CA ALA A 165 -60.120 -1.151 51.482 1.00 44.74 A C ANISOU 1175 CA ALA A 165 4717 6324 5958 -1555 289 1742 A C ATOM 1176 C ALA A 165 -59.372 -1.487 50.200 1.00 45.25 A C ANISOU 1176 C ALA A 165 4800 6168 6223 -1300 267 1797 A C ATOM 1177 O ALA A 165 -58.487 -2.351 50.192 1.00 47.61 A O ANISOU 1177 O ALA A 165 5152 6306 6631 -1285 178 1985 A O ATOM 1178 CB ALA A 165 -61.445 -1.911 51.548 1.00 41.98 A C ANISOU 1178 CB ALA A 165 4378 6044 5528 -1708 336 1642 A C ATOM 1179 N ARG A 166 -59.717 -0.811 49.103 1.00 41.22 A N ANISOU 1179 N ARG A 166 4250 5642 5768 -1105 343 1625 A N ATOM 1180 CA ARG A 166 -58.999 -1.016 47.851 1.00 39.06 A C ANISOU 1180 CA ARG A 166 4005 5172 5665 -880 342 1654 A C ATOM 1181 C ARG A 166 -57.531 -0.638 48.001 1.00 38.43 A C ANISOU 1181 C ARG A 166 3922 5007 5672 -798 297 1791 A C ATOM 1182 O ARG A 166 -56.643 -1.364 47.540 1.00 40.69 A O ANISOU 1182 O ARG A 166 4236 5112 6112 -714 256 1911 A O ATOM 1183 CB ARG A 166 -59.664 -0.209 46.735 1.00 37.67 A C ANISOU 1183 CB ARG A 166 3807 5007 5498 -717 419 1443 A C ATOM 1184 CG ARG A 166 -61.132 -0.550 46.551 1.00 41.68 A C ANISOU 1184 CG ARG A 166 4301 5593 5944 -787 454 1290 A C ATOM 1185 CD ARG A 166 -61.845 0.384 45.586 1.00 45.55 A C ANISOU 1185 CD ARG A 166 4766 6102 6440 -640 497 1074 A C ATOM 1186 NE ARG A 166 -63.282 0.118 45.576 1.00 51.79 A N ANISOU 1186 NE ARG A 166 5516 6983 7178 -723 521 913 A N ATOM 1187 CZ ARG A 166 -64.204 0.979 45.161 1.00 52.06 A C ANISOU 1187 CZ ARG A 166 5495 7089 7197 -658 538 696 A C ATOM 1188 NH1 ARG A 166 -63.844 2.176 44.717 1.00 52.71 A N1+ ANISOU 1188 NH1 ARG A 166 5571 7157 7298 -514 527 624 A N1+ ATOM 1189 NH2 ARG A 166 -65.486 0.643 45.190 1.00 52.37 A N ANISOU 1189 NH2 ARG A 166 5484 7205 7211 -742 556 546 A N ATOM 1190 N ALA A 167 -57.259 0.498 48.647 1.00 39.28 A N ANISOU 1190 N ALA A 167 3987 5242 5695 -823 305 1763 A N ATOM 1191 CA ALA A 167 -55.878 0.894 48.904 1.00 41.08 A C ANISOU 1191 CA ALA A 167 4205 5406 5999 -764 258 1891 A C ATOM 1192 C ALA A 167 -55.127 -0.174 49.695 1.00 42.31 A C ANISOU 1192 C ALA A 167 4391 5470 6215 -881 139 2114 A C ATOM 1193 O ALA A 167 -53.978 -0.498 49.375 1.00 44.96 A O ANISOU 1193 O ALA A 167 4724 5642 6719 -776 88 2225 A O ATOM 1194 CB ALA A 167 -55.848 2.234 49.639 1.00 35.34 A C ANISOU 1194 CB ALA A 167 3430 4851 5146 -809 280 1825 A C ATOM 1195 N GLN A 168 -55.763 -0.741 50.725 1.00 40.70 A N ANISOU 1195 N GLN A 168 4220 5362 5883 -1106 87 2175 A N ATOM 1196 CA GLN A 168 -55.086 -1.737 51.550 1.00 45.53 A C ANISOU 1196 CA GLN A 168 4884 5879 6538 -1241 -58 2400 A C ATOM 1197 C GLN A 168 -54.841 -3.034 50.788 1.00 49.13 A C ANISOU 1197 C GLN A 168 5373 6115 7177 -1156 -109 2480 A C ATOM 1198 O GLN A 168 -53.829 -3.704 51.022 1.00 50.32 A O ANISOU 1198 O GLN A 168 5539 6106 7473 -1148 -237 2654 A O ATOM 1199 CB GLN A 168 -55.893 -1.998 52.822 1.00 52.06 A C ANISOU 1199 CB GLN A 168 5761 6867 7152 -1533 -94 2436 A C ATOM 1200 CG GLN A 168 -55.871 -0.829 53.798 1.00 56.60 A C ANISOU 1200 CG GLN A 168 6306 7639 7560 -1649 -69 2395 A C ATOM 1201 CD GLN A 168 -57.171 -0.674 54.564 1.00 62.10 A C ANISOU 1201 CD GLN A 168 7013 8552 8029 -1886 6 2272 A C ATOM 1202 NE2 GLN A 168 -57.384 0.508 55.133 1.00 61.16 A N ANISOU 1202 NE2 GLN A 168 6840 8618 7779 -1945 76 2155 A N ATOM 1203 OE1 GLN A 168 -57.980 -1.601 54.635 1.00 65.85 A O ANISOU 1203 OE1 GLN A 168 7538 9028 8453 -2018 7 2270 A O ATOM 1204 N VAL A 169 -55.740 -3.402 49.875 1.00 48.40 A N ANISOU 1204 N VAL A 169 5289 6005 7094 -1091 -20 2351 A N ATOM 1205 CA VAL A 169 -55.491 -4.568 49.032 1.00 44.68 A C ANISOU 1205 CA VAL A 169 4847 5323 6807 -994 -52 2406 A C ATOM 1206 C VAL A 169 -54.260 -4.335 48.167 1.00 43.30 A C ANISOU 1206 C VAL A 169 4625 4981 6844 -770 -39 2415 A C ATOM 1207 O VAL A 169 -53.366 -5.186 48.081 1.00 42.09 A O ANISOU 1207 O VAL A 169 4472 4638 6883 -728 -133 2542 A O ATOM 1208 CB VAL A 169 -56.731 -4.892 48.182 1.00 43.21 A C ANISOU 1208 CB VAL A 169 4679 5162 6576 -966 50 2248 A C ATOM 1209 CG1 VAL A 169 -56.352 -5.789 47.017 1.00 42.78 A C ANISOU 1209 CG1 VAL A 169 4641 4886 6727 -808 55 2259 A C ATOM 1210 CG2 VAL A 169 -57.795 -5.548 49.047 1.00 40.49 A C ANISOU 1210 CG2 VAL A 169 4384 4928 6072 -1209 18 2272 A C ATOM 1211 N CYS A 170 -54.198 -3.176 47.507 1.00 43.36 A N ANISOU 1211 N CYS A 170 4594 5052 6830 -632 75 2269 A N ATOM 1212 CA CYS A 170 -53.040 -2.862 46.680 1.00 45.84 A C ANISOU 1212 CA CYS A 170 4870 5224 7324 -443 109 2258 A C ATOM 1213 C CYS A 170 -51.774 -2.752 47.522 1.00 48.48 A C ANISOU 1213 C CYS A 170 5160 5510 7750 -467 -0 2412 A C ATOM 1214 O CYS A 170 -50.683 -3.084 47.046 1.00 50.28 A O ANISOU 1214 O CYS A 170 5347 5562 8194 -351 -21 2455 A O ATOM 1215 CB CYS A 170 -53.289 -1.575 45.891 1.00 45.85 A C ANISOU 1215 CB CYS A 170 4861 5311 7248 -322 241 2077 A C ATOM 1216 SG CYS A 170 -54.626 -1.698 44.673 1.00 46.45 A S ANISOU 1216 SG CYS A 170 4992 5396 7262 -258 346 1890 A S ATOM 1217 N GLN A 171 -51.896 -2.292 48.771 1.00 48.41 A N ANISOU 1217 N GLN A 171 5154 5652 7588 -624 -71 2486 A N ATOM 1218 CA GLN A 171 -50.728 -2.231 49.644 1.00 48.71 A C ANISOU 1218 CA GLN A 171 5160 5641 7706 -665 -200 2646 A C ATOM 1219 C GLN A 171 -50.280 -3.624 50.062 1.00 46.65 A C ANISOU 1219 C GLN A 171 4926 5203 7594 -737 -369 2827 A C ATOM 1220 O GLN A 171 -49.081 -3.924 50.071 1.00 41.84 A O ANISOU 1220 O GLN A 171 4266 4430 7200 -660 -466 2924 A O ATOM 1221 CB GLN A 171 -51.037 -1.394 50.882 1.00 47.79 A C ANISOU 1221 CB GLN A 171 5056 5735 7365 -836 -231 2674 A C ATOM 1222 CG GLN A 171 -49.849 -1.219 51.805 1.00 48.87 A C ANISOU 1222 CG GLN A 171 5168 5834 7566 -886 -371 2836 A C ATOM 1223 CD GLN A 171 -50.251 -0.696 53.169 1.00 50.80 A C ANISOU 1223 CD GLN A 171 5453 6276 7573 -1111 -424 2891 A C ATOM 1224 NE2 GLN A 171 -49.289 -0.140 53.898 1.00 41.26 A N ANISOU 1224 NE2 GLN A 171 4218 5078 6380 -1138 -512 2989 A N ATOM 1225 OE1 GLN A 171 -51.414 -0.791 53.565 1.00 52.49 A O ANISOU 1225 OE1 GLN A 171 5719 6632 7591 -1267 -381 2837 A O ATOM 1226 N GLN A 172 -51.231 -4.485 50.419 1.00 46.69 A N ANISOU 1226 N GLN A 172 5008 5234 7498 -888 -414 2870 A N ATOM 1227 CA GLN A 172 -50.899 -5.866 50.746 1.00 49.39 A C ANISOU 1227 CA GLN A 172 5394 5392 7981 -959 -586 3040 A C ATOM 1228 C GLN A 172 -50.204 -6.549 49.577 1.00 49.36 A C ANISOU 1228 C GLN A 172 5334 5150 8270 -750 -569 3008 A C ATOM 1229 O GLN A 172 -49.251 -7.314 49.769 1.00 50.91 A O ANISOU 1229 O GLN A 172 5505 5149 8690 -725 -725 3140 A O ATOM 1230 CB GLN A 172 -52.166 -6.616 51.153 1.00 52.82 A C ANISOU 1230 CB GLN A 172 5928 5904 8238 -1154 -601 3057 A C ATOM 1231 CG GLN A 172 -51.933 -8.004 51.717 1.00 59.98 A C ANISOU 1231 CG GLN A 172 6911 6638 9239 -1281 -806 3255 A C ATOM 1232 CD GLN A 172 -50.952 -8.002 52.874 1.00 65.07 A C ANISOU 1232 CD GLN A 172 7573 7270 9882 -1357 -1005 3371 A C ATOM 1233 NE2 GLN A 172 -50.075 -9.001 52.904 1.00 64.30 A N ANISOU 1233 NE2 GLN A 172 7468 6966 9996 -1293 -1180 3444 A N ATOM 1234 OE1 GLN A 172 -50.987 -7.121 53.734 1.00 67.45 A O ANISOU 1234 OE1 GLN A 172 7887 7744 9997 -1475 -1004 3382 A O ATOM 1235 N ALA A 173 -50.665 -6.281 48.354 1.00 50.17 A N ANISOU 1235 N ALA A 173 5417 5264 8383 -606 -385 2826 A N ATOM 1236 CA ALA A 173 -50.037 -6.874 47.179 1.00 50.02 A C ANISOU 1236 CA ALA A 173 5349 5031 8624 -422 -338 2768 A C ATOM 1237 C ALA A 173 -48.568 -6.477 47.081 1.00 51.37 A C ANISOU 1237 C ALA A 173 5420 5087 9012 -296 -367 2790 A C ATOM 1238 O ALA A 173 -47.700 -7.326 46.848 1.00 54.57 A O ANISOU 1238 O ALA A 173 5771 5274 9689 -223 -453 2846 A O ATOM 1239 CB ALA A 173 -50.794 -6.466 45.914 1.00 45.47 A C ANISOU 1239 CB ALA A 173 4790 4508 7979 -310 -134 2564 A C ATOM 1240 N GLU A 174 -48.265 -5.188 47.256 1.00 49.47 A N ANISOU 1240 N GLU A 174 5145 4985 8668 -269 -296 2736 A N ATOM 1241 CA GLU A 174 -46.873 -4.752 47.187 1.00 51.17 A C ANISOU 1241 CA GLU A 174 5259 5102 9081 -159 -315 2747 A C ATOM 1242 C GLU A 174 -46.031 -5.401 48.279 1.00 52.40 A C ANISOU 1242 C GLU A 174 5382 5142 9385 -239 -553 2948 A C ATOM 1243 O GLU A 174 -44.858 -5.724 48.058 1.00 53.73 A O ANISOU 1243 O GLU A 174 5451 5134 9829 -134 -613 2957 A O ATOM 1244 CB GLU A 174 -46.781 -3.229 47.271 1.00 53.62 A C ANISOU 1244 CB GLU A 174 5553 5593 9227 -137 -207 2662 A C ATOM 1245 CG GLU A 174 -45.377 -2.701 47.013 1.00 59.09 A C ANISOU 1245 CG GLU A 174 6139 6191 10119 -15 -188 2638 A C ATOM 1246 CD GLU A 174 -45.359 -1.287 46.456 1.00 61.57 A C ANISOU 1246 CD GLU A 174 6453 6637 10304 59 -13 2489 A C ATOM 1247 OE1 GLU A 174 -46.429 -0.787 46.049 1.00 60.97 A O ANISOU 1247 OE1 GLU A 174 6454 6693 10018 46 97 2384 A O ATOM 1248 OE2 GLU A 174 -44.265 -0.681 46.419 1.00 62.08 A O1- ANISOU 1248 OE2 GLU A 174 6437 6663 10485 128 5 2473 A O1- ATOM 1249 N HIS A 175 -46.606 -5.596 49.466 1.00 51.81 A N ANISOU 1249 N HIS A 175 5389 5169 9126 -434 -695 3091 A N ATOM 1250 CA HIS A 175 -45.864 -6.245 50.543 1.00 52.04 A C ANISOU 1250 CA HIS A 175 5416 5125 9231 -527 -939 3229 A C ATOM 1251 C HIS A 175 -45.538 -7.691 50.191 1.00 47.81 A C ANISOU 1251 C HIS A 175 4865 4382 8919 -478 -1049 3227 A C ATOM 1252 O HIS A 175 -44.370 -8.098 50.186 1.00 54.72 A O ANISOU 1252 O HIS A 175 5643 5106 10042 -394 -1158 3223 A O ATOM 1253 CB HIS A 175 -46.656 -6.190 51.852 1.00 54.08 A C ANISOU 1253 CB HIS A 175 5794 5558 9194 -771 -1048 3340 A C ATOM 1254 CG HIS A 175 -46.657 -4.849 52.517 1.00 59.90 A C ANISOU 1254 CG HIS A 175 6530 6492 9738 -844 -1000 3354 A C ATOM 1255 CD2 HIS A 175 -46.391 -3.610 52.040 1.00 59.55 A C ANISOU 1255 CD2 HIS A 175 6414 6528 9685 -732 -842 3265 A C ATOM 1256 ND1 HIS A 175 -46.993 -4.684 53.844 1.00 61.61 A N ANISOU 1256 ND1 HIS A 175 6833 6860 9714 -1065 -1114 3439 A N ATOM 1257 CE1 HIS A 175 -46.917 -3.405 54.160 1.00 60.87 A C ANISOU 1257 CE1 HIS A 175 6712 6927 9490 -1084 -1031 3415 A C ATOM 1258 NE2 HIS A 175 -46.557 -2.730 53.083 1.00 59.74 A N ANISOU 1258 NE2 HIS A 175 6472 6746 9482 -879 -870 3308 A N ATOM 1259 N SER A 176 -46.567 -8.480 49.874 1.00 53.16 A N ANISOU 1259 N SER A 176 5629 5049 9520 -532 -1018 3218 A N ATOM 1260 CA SER A 176 -46.406 -9.927 49.783 1.00 56.00 A C ANISOU 1260 CA SER A 176 6001 5233 10044 -531 -1155 3241 A C ATOM 1261 C SER A 176 -45.815 -10.382 48.455 1.00 56.17 A C ANISOU 1261 C SER A 176 5915 5072 10354 -324 -1048 3102 A C ATOM 1262 O SER A 176 -45.072 -11.369 48.424 1.00 56.91 A O ANISOU 1262 O SER A 176 5953 4994 10676 -281 -1180 3103 A O ATOM 1263 CB SER A 176 -47.753 -10.612 50.020 1.00 60.93 A C ANISOU 1263 CB SER A 176 6766 5923 10461 -687 -1166 3287 A C ATOM 1264 OG SER A 176 -48.261 -10.298 51.306 1.00 63.66 A O ANISOU 1264 OG SER A 176 7214 6439 10535 -907 -1264 3396 A O ATOM 1265 N PHE A 177 -46.127 -9.700 47.356 1.00 57.82 A N ANISOU 1265 N PHE A 177 6099 5314 10557 -206 -811 2972 A N ATOM 1266 CA PHE A 177 -45.689 -10.161 46.044 1.00 59.13 A C ANISOU 1266 CA PHE A 177 6186 5320 10960 -36 -684 2817 A C ATOM 1267 C PHE A 177 -44.505 -9.388 45.487 1.00 56.45 A C ANISOU 1267 C PHE A 177 5715 4935 10799 108 -579 2705 A C ATOM 1268 O PHE A 177 -43.766 -9.931 44.660 1.00 55.66 A O ANISOU 1268 O PHE A 177 5523 4683 10944 220 -526 2582 A O ATOM 1269 CB PHE A 177 -46.846 -10.112 45.043 1.00 58.90 A C ANISOU 1269 CB PHE A 177 6235 5329 10814 -9 -487 2725 A C ATOM 1270 CG PHE A 177 -47.727 -11.326 45.087 1.00 61.43 A C ANISOU 1270 CG PHE A 177 6645 5601 11095 -94 -563 2770 A C ATOM 1271 CD1 PHE A 177 -48.671 -11.486 46.087 1.00 62.11 A C ANISOU 1271 CD1 PHE A 177 6841 5807 10949 -280 -671 2904 A C ATOM 1272 CD2 PHE A 177 -47.594 -12.320 44.133 1.00 63.12 A C ANISOU 1272 CD2 PHE A 177 6833 5653 11498 -2 -519 2669 A C ATOM 1273 CE1 PHE A 177 -49.474 -12.609 46.125 1.00 63.28 A C ANISOU 1273 CE1 PHE A 177 7076 5910 11056 -369 -735 2940 A C ATOM 1274 CE2 PHE A 177 -48.391 -13.443 44.166 1.00 63.42 A C ANISOU 1274 CE2 PHE A 177 6955 5642 11502 -79 -590 2711 A C ATOM 1275 CZ PHE A 177 -49.334 -13.588 45.162 1.00 63.02 A C ANISOU 1275 CZ PHE A 177 7017 5707 11221 -262 -699 2850 A C ATOM 1276 N ALA A 178 -44.301 -8.141 45.907 1.00 55.19 A N ANISOU 1276 N ALA A 178 5542 4905 10522 97 -539 2733 A N ATOM 1277 CA ALA A 178 -43.143 -7.375 45.468 1.00 54.86 A C ANISOU 1277 CA ALA A 178 5378 4825 10640 217 -446 2631 A C ATOM 1278 C ALA A 178 -42.039 -7.308 46.516 1.00 56.97 A C ANISOU 1278 C ALA A 178 5558 5069 11018 179 -642 2723 A C ATOM 1279 O ALA A 178 -40.942 -6.832 46.204 1.00 57.84 A O ANISOU 1279 O ALA A 178 5548 5125 11302 270 -586 2635 A O ATOM 1280 CB ALA A 178 -43.560 -5.952 45.075 1.00 52.77 A C ANISOU 1280 CB ALA A 178 5153 4705 10192 251 -253 2578 A C ATOM 1281 N GLY A 179 -42.295 -7.775 47.736 1.00 56.08 A N ANISOU 1281 N GLY A 179 5510 4993 10805 35 -866 2889 A N ATOM 1282 CA GLY A 179 -41.285 -7.732 48.775 1.00 57.81 A C ANISOU 1282 CA GLY A 179 5665 5185 11116 -16 -1072 2982 A C ATOM 1283 C GLY A 179 -40.905 -6.329 49.183 1.00 54.25 A C ANISOU 1283 C GLY A 179 5184 4870 10559 -18 -1018 3000 A C ATOM 1284 O GLY A 179 -39.769 -6.097 49.609 1.00 59.18 A O ANISOU 1284 O GLY A 179 5706 5442 11336 3 -1116 3010 A O ATOM 1285 N MET A 180 -41.831 -5.383 49.060 1.00 53.24 A N ANISOU 1285 N MET A 180 5141 4913 10177 -45 -867 3000 A N ATOM 1286 CA MET A 180 -41.575 -3.973 49.349 1.00 54.81 A C ANISOU 1286 CA MET A 180 5318 5251 10257 -41 -792 3005 A C ATOM 1287 C MET A 180 -42.553 -3.500 50.416 1.00 55.19 A C ANISOU 1287 C MET A 180 5492 5499 9978 -223 -856 3134 A C ATOM 1288 O MET A 180 -43.735 -3.253 50.115 1.00 56.32 A O ANISOU 1288 O MET A 180 5725 5761 9911 -265 -727 3099 A O ATOM 1289 CB MET A 180 -41.713 -3.148 48.069 1.00 58.27 A C ANISOU 1289 CB MET A 180 5733 5704 10703 102 -522 2849 A C ATOM 1290 CG MET A 180 -41.852 -1.646 48.250 1.00 63.51 A C ANISOU 1290 CG MET A 180 6419 6584 11126 85 -404 2790 A C ATOM 1291 SD MET A 180 -40.357 -0.844 48.854 1.00 68.15 A S ANISOU 1291 SD MET A 180 6879 7148 11865 120 -483 2834 A S ATOM 1292 CE MET A 180 -41.066 0.289 50.039 1.00 66.50 A C ANISOU 1292 CE MET A 180 6767 7218 11280 -41 -519 2915 A C ATOM 1293 N PRO A 181 -42.120 -3.359 51.668 1.00 55.21 A N ANISOU 1293 N PRO A 181 5504 5559 9915 -348 -1043 3255 A N ATOM 1294 CA PRO A 181 -43.034 -2.981 52.767 1.00 53.64 A C ANISOU 1294 CA PRO A 181 5431 5561 9389 -554 -1101 3357 A C ATOM 1295 C PRO A 181 -43.311 -1.483 52.777 1.00 49.87 A C ANISOU 1295 C PRO A 181 4953 5271 8723 -556 -941 3319 A C ATOM 1296 O PRO A 181 -42.845 -0.718 53.630 1.00 50.90 A O ANISOU 1296 O PRO A 181 5072 5500 8767 -627 -1008 3375 A O ATOM 1297 CB PRO A 181 -42.266 -3.454 54.004 1.00 54.68 A C ANISOU 1297 CB PRO A 181 5567 5647 9560 -674 -1367 3482 A C ATOM 1298 CG PRO A 181 -40.834 -3.272 53.621 1.00 55.65 A C ANISOU 1298 CG PRO A 181 5535 5624 9984 -513 -1391 3434 A C ATOM 1299 CD PRO A 181 -40.744 -3.581 52.145 1.00 54.23 A C ANISOU 1299 CD PRO A 181 5275 5312 10017 -318 -1212 3288 A C ATOM 1300 N CYS A 182 -44.096 -1.042 51.800 1.00 45.87 A N ANISOU 1300 N CYS A 182 4461 4855 8113 -472 -717 3142 A N ATOM 1301 CA CYS A 182 -44.414 0.367 51.652 1.00 44.62 A C ANISOU 1301 CA CYS A 182 4301 4897 7754 -448 -550 3009 A C ATOM 1302 C CYS A 182 -45.511 0.790 52.626 1.00 43.10 A C ANISOU 1302 C CYS A 182 4200 4931 7245 -646 -560 3033 A C ATOM 1303 O CYS A 182 -46.139 -0.029 53.302 1.00 44.00 A O ANISOU 1303 O CYS A 182 4392 5057 7270 -809 -667 3136 A O ATOM 1304 CB CYS A 182 -44.856 0.663 50.223 1.00 45.84 A C ANISOU 1304 CB CYS A 182 4451 5047 7921 -291 -332 2808 A C ATOM 1305 SG CYS A 182 -46.382 -0.191 49.756 1.00 48.71 A S ANISOU 1305 SG CYS A 182 4911 5436 8160 -345 -275 2751 A S ATOM 1306 N GLY A 183 -45.738 2.102 52.687 1.00 45.37 A N ANISOU 1306 N GLY A 183 4479 5398 7364 -638 -441 2924 A N ATOM 1307 CA GLY A 183 -46.880 2.644 53.386 1.00 47.03 A C ANISOU 1307 CA GLY A 183 4752 5831 7285 -800 -399 2878 A C ATOM 1308 C GLY A 183 -48.089 2.739 52.473 1.00 48.26 A C ANISOU 1308 C GLY A 183 4936 6053 7348 -742 -237 2699 A C ATOM 1309 O GLY A 183 -48.073 2.311 51.320 1.00 51.58 A O ANISOU 1309 O GLY A 183 5346 6344 7909 -591 -166 2627 A O ATOM 1310 N ILE A 184 -49.161 3.326 53.012 1.00 50.93 A N ANISOU 1310 N ILE A 184 5306 6596 7449 -870 -180 2615 A N ATOM 1311 CA ILE A 184 -50.418 3.418 52.270 1.00 50.59 A C ANISOU 1311 CA ILE A 184 5282 6623 7316 -834 -50 2439 A C ATOM 1312 C ILE A 184 -50.475 4.604 51.323 1.00 51.04 A C ANISOU 1312 C ILE A 184 5305 6716 7370 -660 85 2258 A C ATOM 1313 O ILE A 184 -51.394 4.678 50.499 1.00 52.12 A O ANISOU 1313 O ILE A 184 5460 6871 7474 -593 175 2110 A O ATOM 1314 CB ILE A 184 -51.615 3.526 53.231 1.00 53.34 A C ANISOU 1314 CB ILE A 184 5663 7174 7431 -1052 -40 2394 A C ATOM 1315 CG1 ILE A 184 -51.353 4.602 54.291 1.00 53.95 A C ANISOU 1315 CG1 ILE A 184 5719 7414 7366 -1163 -53 2400 A C ATOM 1316 CG2 ILE A 184 -51.880 2.184 53.897 1.00 56.83 A C ANISOU 1316 CG2 ILE A 184 6171 7567 7854 -1234 -153 2544 A C ATOM 1317 CD1 ILE A 184 -51.481 6.041 53.783 1.00 52.29 A C ANISOU 1317 CD1 ILE A 184 5453 7299 7115 -1029 67 2216 A C ATOM 1318 N MET A 185 -49.513 5.524 51.409 1.00 51.14 A N ANISOU 1318 N MET A 185 5280 6733 7420 -590 88 2269 A N ATOM 1319 CA MET A 185 -49.648 6.810 50.731 1.00 49.38 A C ANISOU 1319 CA MET A 185 5043 6572 7147 -467 200 2103 A C ATOM 1320 C MET A 185 -49.885 6.650 49.234 1.00 47.59 A C ANISOU 1320 C MET A 185 4847 6224 7013 -300 291 1986 A C ATOM 1321 O MET A 185 -50.855 7.189 48.688 1.00 47.10 A O ANISOU 1321 O MET A 185 4809 6228 6857 -261 361 1829 A O ATOM 1322 CB MET A 185 -48.418 7.673 50.995 1.00 47.40 A C ANISOU 1322 CB MET A 185 4751 6313 6946 -418 185 2152 A C ATOM 1323 CG MET A 185 -48.381 8.913 50.144 1.00 47.13 A C ANISOU 1323 CG MET A 185 4721 6301 6887 -281 291 1996 A C ATOM 1324 SD MET A 185 -46.807 9.765 50.205 1.00 51.49 A S ANISOU 1324 SD MET A 185 5227 6803 7534 -206 289 2051 A S ATOM 1325 CE MET A 185 -47.367 11.330 49.569 1.00 51.99 A C ANISOU 1325 CE MET A 185 5326 6963 7464 -123 394 1852 A C ATOM 1326 N ASP A 186 -49.005 5.921 48.548 1.00 46.14 A N ANISOU 1326 N ASP A 186 4659 5855 7017 -203 287 2052 A N ATOM 1327 CA ASP A 186 -49.063 5.899 47.090 1.00 41.97 A C ANISOU 1327 CA ASP A 186 4171 5210 6568 -54 387 1934 A C ATOM 1328 C ASP A 186 -50.387 5.332 46.599 1.00 42.71 A C ANISOU 1328 C ASP A 186 4316 5317 6594 -70 414 1849 A C ATOM 1329 O ASP A 186 -51.019 5.893 45.697 1.00 42.35 A O ANISOU 1329 O ASP A 186 4319 5281 6492 9 487 1701 A O ATOM 1330 CB ASP A 186 -47.890 5.101 46.526 1.00 46.73 A C ANISOU 1330 CB ASP A 186 4745 5612 7398 29 386 2007 A C ATOM 1331 CG ASP A 186 -46.553 5.743 46.828 1.00 51.62 A C ANISOU 1331 CG ASP A 186 5302 6206 8107 64 375 2059 A C ATOM 1332 OD1 ASP A 186 -46.526 6.959 47.121 1.00 54.47 A O ANISOU 1332 OD1 ASP A 186 5664 6688 8345 58 401 2010 A O ATOM 1333 OD2 ASP A 186 -45.529 5.032 46.770 1.00 51.97 A O1- ANISOU 1333 OD2 ASP A 186 5288 6102 8355 99 337 2140 A O1- ATOM 1334 N GLN A 187 -50.824 4.213 47.180 1.00 40.82 A N ANISOU 1334 N GLN A 187 4074 5073 6361 -177 344 1941 A N ATOM 1335 CA GLN A 187 -52.106 3.636 46.789 1.00 38.00 A C ANISOU 1335 CA GLN A 187 3760 4739 5941 -206 368 1859 A C ATOM 1336 C GLN A 187 -53.247 4.601 47.074 1.00 38.51 A C ANISOU 1336 C GLN A 187 3822 4989 5822 -256 400 1716 A C ATOM 1337 O GLN A 187 -54.195 4.711 46.286 1.00 39.56 A O ANISOU 1337 O GLN A 187 3986 5127 5918 -203 449 1575 A O ATOM 1338 CB GLN A 187 -52.336 2.315 47.521 1.00 37.48 A C ANISOU 1338 CB GLN A 187 3697 4646 5898 -341 279 1994 A C ATOM 1339 CG GLN A 187 -51.331 1.229 47.193 1.00 39.96 A C ANISOU 1339 CG GLN A 187 4005 4753 6424 -285 227 2121 A C ATOM 1340 CD GLN A 187 -50.009 1.440 47.906 1.00 41.32 A C ANISOU 1340 CD GLN A 187 4124 4884 6690 -294 147 2255 A C ATOM 1341 NE2 GLN A 187 -48.966 0.778 47.425 1.00 39.79 A N ANISOU 1341 NE2 GLN A 187 3899 4499 6723 -201 121 2318 A N ATOM 1342 OE1 GLN A 187 -49.929 2.187 48.882 1.00 42.02 A O ANISOU 1342 OE1 GLN A 187 4194 5111 6659 -386 107 2291 A O ATOM 1343 N PHE A 188 -53.168 5.312 48.199 1.00 37.21 A N ANISOU 1343 N PHE A 188 3616 4972 5551 -361 369 1742 A N ATOM 1344 CA PHE A 188 -54.262 6.179 48.617 1.00 42.20 A C ANISOU 1344 CA PHE A 188 4224 5785 6025 -427 398 1593 A C ATOM 1345 C PHE A 188 -54.457 7.327 47.638 1.00 39.85 A C ANISOU 1345 C PHE A 188 3940 5479 5723 -272 456 1427 A C ATOM 1346 O PHE A 188 -55.586 7.632 47.237 1.00 40.33 A O ANISOU 1346 O PHE A 188 4003 5593 5729 -253 479 1266 A O ATOM 1347 CB PHE A 188 -53.971 6.733 50.012 1.00 51.19 A C ANISOU 1347 CB PHE A 188 5319 7073 7059 -575 360 1656 A C ATOM 1348 CG PHE A 188 -55.193 6.952 50.847 1.00 58.68 A C ANISOU 1348 CG PHE A 188 6235 8212 7850 -739 378 1547 A C ATOM 1349 CD1 PHE A 188 -56.004 8.056 50.646 1.00 61.72 A C ANISOU 1349 CD1 PHE A 188 6578 8705 8166 -695 434 1339 A C ATOM 1350 CD2 PHE A 188 -55.505 6.073 51.869 1.00 63.52 A C ANISOU 1350 CD2 PHE A 188 6858 8890 8386 -949 336 1644 A C ATOM 1351 CE1 PHE A 188 -57.128 8.254 51.422 1.00 65.33 A C ANISOU 1351 CE1 PHE A 188 6983 9338 8501 -851 463 1210 A C ATOM 1352 CE2 PHE A 188 -56.621 6.270 52.654 1.00 67.08 A C ANISOU 1352 CE2 PHE A 188 7276 9524 8687 -1125 374 1524 A C ATOM 1353 CZ PHE A 188 -57.434 7.362 52.431 1.00 67.25 A C ANISOU 1353 CZ PHE A 188 7233 9658 8659 -1073 446 1297 A C ATOM 1354 N ILE A 189 -53.359 7.973 47.234 1.00 38.32 A N ANISOU 1354 N ILE A 189 3760 5209 5590 -165 470 1461 A N ATOM 1355 CA ILE A 189 -53.462 9.134 46.355 1.00 40.75 A C ANISOU 1355 CA ILE A 189 4104 5501 5877 -37 511 1317 A C ATOM 1356 C ILE A 189 -53.851 8.728 44.938 1.00 43.05 A C ANISOU 1356 C ILE A 189 4477 5653 6228 75 544 1238 A C ATOM 1357 O ILE A 189 -54.590 9.454 44.262 1.00 40.32 A O ANISOU 1357 O ILE A 189 4173 5314 5832 141 547 1088 A O ATOM 1358 CB ILE A 189 -52.153 9.946 46.368 1.00 29.63 A C ANISOU 1358 CB ILE A 189 2695 4057 4504 21 523 1376 A C ATOM 1359 CG1 ILE A 189 -52.290 11.172 45.461 1.00 28.86 A C ANISOU 1359 CG1 ILE A 189 2659 3938 4368 135 555 1231 A C ATOM 1360 CG2 ILE A 189 -50.972 9.090 45.920 1.00 29.92 A C ANISOU 1360 CG2 ILE A 189 2745 3931 4693 70 538 1504 A C ATOM 1361 CD1 ILE A 189 -53.469 12.066 45.803 1.00 28.70 A C ANISOU 1361 CD1 ILE A 189 2614 4056 4235 109 527 1077 A C ATOM 1362 N SER A 190 -53.371 7.578 44.459 1.00 44.37 A N ANISOU 1362 N SER A 190 4670 5682 6505 96 558 1332 A N ATOM 1363 CA SER A 190 -53.748 7.132 43.120 1.00 40.51 A C ANISOU 1363 CA SER A 190 4265 5061 6064 186 596 1256 A C ATOM 1364 C SER A 190 -55.251 6.906 43.014 1.00 38.59 A C ANISOU 1364 C SER A 190 4028 4883 5749 153 571 1142 A C ATOM 1365 O SER A 190 -55.853 7.157 41.964 1.00 29.58 A O ANISOU 1365 O SER A 190 2963 3681 4596 232 580 1021 A O ATOM 1366 CB SER A 190 -52.989 5.854 42.762 1.00 38.85 A C ANISOU 1366 CB SER A 190 4063 4699 5999 199 617 1370 A C ATOM 1367 OG SER A 190 -53.043 5.595 41.369 1.00 40.44 A O ANISOU 1367 OG SER A 190 4357 4759 6250 291 676 1293 A O ATOM 1368 N LEU A 191 -55.875 6.428 44.090 1.00 40.42 A N ANISOU 1368 N LEU A 191 4187 5237 5933 25 537 1174 A N ATOM 1369 CA LEU A 191 -57.321 6.233 44.095 1.00 37.65 A C ANISOU 1369 CA LEU A 191 3819 4965 5521 -23 523 1047 A C ATOM 1370 C LEU A 191 -58.068 7.515 44.437 1.00 41.11 A C ANISOU 1370 C LEU A 191 4209 5543 5868 -27 506 887 A C ATOM 1371 O LEU A 191 -59.187 7.726 43.953 1.00 46.18 A O ANISOU 1371 O LEU A 191 4851 6203 6493 3 490 727 A O ATOM 1372 CB LEU A 191 -57.702 5.119 45.070 1.00 35.27 A C ANISOU 1372 CB LEU A 191 3469 4732 5202 -182 505 1137 A C ATOM 1373 CG LEU A 191 -57.486 3.691 44.567 1.00 35.95 A C ANISOU 1373 CG LEU A 191 3603 4671 5386 -177 505 1243 A C ATOM 1374 CD1 LEU A 191 -56.633 2.899 45.538 1.00 37.49 A C ANISOU 1374 CD1 LEU A 191 3776 4851 5620 -283 463 1441 A C ATOM 1375 CD2 LEU A 191 -58.835 3.015 44.356 1.00 36.36 A C ANISOU 1375 CD2 LEU A 191 3657 4754 5406 -231 506 1146 A C ATOM 1376 N MET A 192 -57.469 8.375 45.259 1.00 41.63 A N ANISOU 1376 N MET A 192 4229 5701 5888 -61 503 918 A N ATOM 1377 CA MET A 192 -58.179 9.461 45.917 1.00 44.12 A C ANISOU 1377 CA MET A 192 4470 6173 6120 -105 490 773 A C ATOM 1378 C MET A 192 -57.873 10.822 45.312 1.00 40.62 A C ANISOU 1378 C MET A 192 4064 5693 5676 26 472 683 A C ATOM 1379 O MET A 192 -58.470 11.819 45.732 1.00 36.84 A O ANISOU 1379 O MET A 192 3524 5324 5150 13 451 542 A O ATOM 1380 CB MET A 192 -57.826 9.485 47.410 1.00 51.74 A C ANISOU 1380 CB MET A 192 5358 7286 7013 -267 496 863 A C ATOM 1381 CG MET A 192 -58.412 8.346 48.223 1.00 63.77 A C ANISOU 1381 CG MET A 192 6847 8886 8496 -443 500 915 A C ATOM 1382 SD MET A 192 -60.171 8.570 48.533 1.00 77.24 A S ANISOU 1382 SD MET A 192 8464 10749 10136 -536 524 668 A S ATOM 1383 CE MET A 192 -60.135 10.042 49.559 1.00 78.51 A C ANISOU 1383 CE MET A 192 8535 11086 10210 -599 537 560 A C ATOM 1384 N GLY A 193 -56.973 10.895 44.336 1.00 38.64 A N ANISOU 1384 N GLY A 193 3914 5289 5479 140 483 749 A N ATOM 1385 CA GLY A 193 -56.606 12.186 43.789 1.00 38.37 A C ANISOU 1385 CA GLY A 193 3937 5215 5429 241 465 678 A C ATOM 1386 C GLY A 193 -57.785 12.879 43.135 1.00 39.93 A C ANISOU 1386 C GLY A 193 4160 5402 5610 309 401 482 A C ATOM 1387 O GLY A 193 -58.678 12.245 42.568 1.00 41.49 A O ANISOU 1387 O GLY A 193 4376 5555 5834 323 379 413 A O ATOM 1388 N GLN A 194 -57.782 14.205 43.220 1.00 40.03 A N ANISOU 1388 N GLN A 194 4170 5449 5589 352 357 389 A N ATOM 1389 CA GLN A 194 -58.749 15.042 42.527 1.00 39.46 A C ANISOU 1389 CA GLN A 194 4135 5334 5523 436 264 204 A C ATOM 1390 C GLN A 194 -57.969 16.134 41.815 1.00 38.63 A C ANISOU 1390 C GLN A 194 4157 5123 5396 525 231 211 A C ATOM 1391 O GLN A 194 -57.072 16.739 42.411 1.00 39.67 A O ANISOU 1391 O GLN A 194 4266 5309 5498 504 266 280 A O ATOM 1392 CB GLN A 194 -59.769 15.636 43.504 1.00 41.76 A C ANISOU 1392 CB GLN A 194 4272 5789 5807 380 226 41 A C ATOM 1393 CG GLN A 194 -60.534 14.580 44.298 1.00 48.44 A C ANISOU 1393 CG GLN A 194 4995 6755 6654 257 276 27 A C ATOM 1394 CD GLN A 194 -61.501 13.785 43.441 1.00 55.82 A C ANISOU 1394 CD GLN A 194 5962 7606 7640 293 240 -48 A C ATOM 1395 NE2 GLN A 194 -61.930 12.631 43.945 1.00 57.38 A N ANISOU 1395 NE2 GLN A 194 6093 7873 7835 184 297 -12 A N ATOM 1396 OE1 GLN A 194 -61.856 14.201 42.337 1.00 58.06 A O ANISOU 1396 OE1 GLN A 194 6340 7760 7961 409 156 -134 A O ATOM 1397 N LYS A 195 -58.297 16.386 40.550 1.00 40.76 A N ANISOU 1397 N LYS A 195 4572 5242 5674 613 159 143 A N ATOM 1398 CA LYS A 195 -57.505 17.330 39.774 1.00 41.09 A C ANISOU 1398 CA LYS A 195 4769 5166 5676 674 132 162 A C ATOM 1399 C LYS A 195 -57.589 18.723 40.387 1.00 40.07 A C ANISOU 1399 C LYS A 195 4588 5112 5526 691 61 72 A C ATOM 1400 O LYS A 195 -58.636 19.138 40.892 1.00 35.64 A O ANISOU 1400 O LYS A 195 3914 4633 4994 695 -19 -75 A O ATOM 1401 CB LYS A 195 -57.969 17.350 38.317 1.00 43.13 A C ANISOU 1401 CB LYS A 195 5214 5244 5929 741 48 99 A C ATOM 1402 CG LYS A 195 -59.036 18.379 37.995 1.00 48.76 A C ANISOU 1402 CG LYS A 195 5955 5919 6651 805 -128 -76 A C ATOM 1403 CD LYS A 195 -58.930 18.800 36.538 1.00 54.94 A C ANISOU 1403 CD LYS A 195 6988 6498 7388 856 -218 -88 A C ATOM 1404 CE LYS A 195 -57.481 19.133 36.193 1.00 59.82 A C ANISOU 1404 CE LYS A 195 7742 7053 7932 830 -118 38 A C ATOM 1405 NZ LYS A 195 -57.320 19.626 34.796 1.00 64.42 A N1+ ANISOU 1405 NZ LYS A 195 8594 7440 8441 846 -197 23 A N1+ ATOM 1406 N GLY A 196 -56.474 19.447 40.337 1.00 38.51 A N ANISOU 1406 N GLY A 196 4465 4884 5284 697 94 148 A N ATOM 1407 CA GLY A 196 -56.393 20.749 40.972 1.00 39.60 A C ANISOU 1407 CA GLY A 196 4555 5094 5399 706 40 81 A C ATOM 1408 C GLY A 196 -56.405 20.717 42.485 1.00 40.34 A C ANISOU 1408 C GLY A 196 4444 5388 5498 628 98 88 A C ATOM 1409 O GLY A 196 -56.791 21.707 43.115 1.00 42.30 A O ANISOU 1409 O GLY A 196 4611 5719 5744 630 39 -25 A O ATOM 1410 N HIS A 197 -55.978 19.609 43.088 1.00 38.99 A N ANISOU 1410 N HIS A 197 4193 5289 5332 550 205 216 A N ATOM 1411 CA HIS A 197 -55.982 19.461 44.536 1.00 36.13 A C ANISOU 1411 CA HIS A 197 3661 5112 4954 445 255 240 A C ATOM 1412 C HIS A 197 -54.801 18.609 44.971 1.00 37.89 A C ANISOU 1412 C HIS A 197 3874 5349 5175 380 352 444 A C ATOM 1413 O HIS A 197 -54.421 17.661 44.280 1.00 40.19 A O ANISOU 1413 O HIS A 197 4235 5532 5505 400 391 539 A O ATOM 1414 CB HIS A 197 -57.267 18.799 45.045 1.00 35.17 A C ANISOU 1414 CB HIS A 197 3418 5091 4855 384 245 134 A C ATOM 1415 CG HIS A 197 -58.483 19.662 44.940 1.00 35.22 A C ANISOU 1415 CG HIS A 197 3373 5117 4891 432 147 -94 A C ATOM 1416 CD2 HIS A 197 -59.094 20.453 45.853 1.00 34.41 A C ANISOU 1416 CD2 HIS A 197 3133 5151 4790 388 125 -246 A C ATOM 1417 ND1 HIS A 197 -59.225 19.766 43.784 1.00 36.19 A N ANISOU 1417 ND1 HIS A 197 3585 5101 5064 535 48 -201 A N ATOM 1418 CE1 HIS A 197 -60.241 20.586 43.989 1.00 37.35 A C ANISOU 1418 CE1 HIS A 197 3644 5290 5258 563 -45 -409 A C ATOM 1419 NE2 HIS A 197 -60.182 21.018 45.235 1.00 36.87 A N ANISOU 1419 NE2 HIS A 197 3438 5398 5173 477 9 -449 A N ATOM 1420 N ALA A 198 -54.230 18.958 46.117 1.00 34.72 A N ANISOU 1420 N ALA A 198 3382 5073 4738 301 382 504 A N ATOM 1421 CA ALA A 198 -53.370 18.058 46.867 1.00 35.41 A C ANISOU 1421 CA ALA A 198 3418 5203 4832 210 442 683 A C ATOM 1422 C ALA A 198 -54.191 17.379 47.958 1.00 28.15 A C ANISOU 1422 C ALA A 198 2383 4433 3882 76 447 668 A C ATOM 1423 O ALA A 198 -55.252 17.862 48.360 1.00 31.59 A O ANISOU 1423 O ALA A 198 2748 4971 4283 42 424 507 A O ATOM 1424 CB ALA A 198 -52.186 18.812 47.477 1.00 34.05 A C ANISOU 1424 CB ALA A 198 3231 5072 4636 188 461 771 A C ATOM 1425 N LEU A 199 -53.683 16.252 48.445 1.00 33.66 A N ANISOU 1425 N LEU A 199 3060 5135 4596 -9 474 830 A N ATOM 1426 CA LEU A 199 -54.392 15.449 49.436 1.00 37.41 A C ANISOU 1426 CA LEU A 199 3456 5734 5026 -162 478 841 A C ATOM 1427 C LEU A 199 -53.581 15.410 50.722 1.00 36.25 A C ANISOU 1427 C LEU A 199 3260 5687 4826 -299 478 982 A C ATOM 1428 O LEU A 199 -52.531 14.763 50.782 1.00 35.14 A O ANISOU 1428 O LEU A 199 3147 5467 4737 -305 467 1164 A O ATOM 1429 CB LEU A 199 -54.668 14.038 48.922 1.00 41.71 A C ANISOU 1429 CB LEU A 199 4035 6185 5628 -166 483 911 A C ATOM 1430 CG LEU A 199 -56.124 13.765 48.551 1.00 51.19 A C ANISOU 1430 CG LEU A 199 5216 7412 6823 -167 480 745 A C ATOM 1431 CD1 LEU A 199 -56.381 12.271 48.508 1.00 53.63 A C ANISOU 1431 CD1 LEU A 199 5539 7677 7161 -234 488 839 A C ATOM 1432 CD2 LEU A 199 -57.047 14.433 49.555 1.00 55.22 A C ANISOU 1432 CD2 LEU A 199 5621 8110 7251 -280 485 590 A C ATOM 1433 N LEU A 200 -54.065 16.112 51.740 1.00 37.60 A N ANISOU 1433 N LEU A 200 3358 6027 4902 -412 484 888 A N ATOM 1434 CA LEU A 200 -53.508 15.997 53.080 1.00 38.91 A C ANISOU 1434 CA LEU A 200 3487 6309 4990 -584 478 1011 A C ATOM 1435 C LEU A 200 -54.071 14.734 53.718 1.00 40.82 A C ANISOU 1435 C LEU A 200 3720 6604 5187 -754 476 1076 A C ATOM 1436 O LEU A 200 -55.260 14.675 54.049 1.00 41.68 A O ANISOU 1436 O LEU A 200 3779 6824 5233 -851 510 926 A O ATOM 1437 CB LEU A 200 -53.845 17.234 53.905 1.00 43.10 A C ANISOU 1437 CB LEU A 200 3948 7001 5426 -656 498 869 A C ATOM 1438 CG LEU A 200 -53.354 17.232 55.353 1.00 43.85 A C ANISOU 1438 CG LEU A 200 4015 7234 5413 -859 493 976 A C ATOM 1439 CD1 LEU A 200 -51.831 17.200 55.434 1.00 43.25 A C ANISOU 1439 CD1 LEU A 200 3985 7069 5381 -821 446 1192 A C ATOM 1440 CD2 LEU A 200 -53.917 18.431 56.101 1.00 42.57 A C ANISOU 1440 CD2 LEU A 200 3776 7239 5159 -936 532 789 A C ATOM 1441 N ILE A 201 -53.225 13.720 53.880 1.00 40.76 A N ANISOU 1441 N ILE A 201 3757 6509 5221 -795 432 1292 A N ATOM 1442 CA ILE A 201 -53.638 12.417 54.386 1.00 41.34 A C ANISOU 1442 CA ILE A 201 3849 6595 5264 -951 408 1386 A C ATOM 1443 C ILE A 201 -53.073 12.236 55.786 1.00 42.42 A C ANISOU 1443 C ILE A 201 3991 6825 5301 -1162 357 1537 A C ATOM 1444 O ILE A 201 -51.857 12.345 55.993 1.00 46.37 A O ANISOU 1444 O ILE A 201 4508 7259 5850 -1132 297 1694 A O ATOM 1445 CB ILE A 201 -53.177 11.270 53.469 1.00 39.11 A C ANISOU 1445 CB ILE A 201 3622 6117 5121 -842 374 1515 A C ATOM 1446 CG1 ILE A 201 -53.642 11.501 52.027 1.00 37.12 A C ANISOU 1446 CG1 ILE A 201 3386 5762 4955 -639 422 1373 A C ATOM 1447 CG2 ILE A 201 -53.693 9.937 53.995 1.00 37.83 A C ANISOU 1447 CG2 ILE A 201 3487 5965 4923 -1009 341 1604 A C ATOM 1448 CD1 ILE A 201 -53.006 10.561 51.014 1.00 36.79 A C ANISOU 1448 CD1 ILE A 201 3400 5518 5059 -515 407 1483 A C ATOM 1449 N ASP A 202 -53.955 11.968 56.744 1.00 42.15 A N ANISOU 1449 N ASP A 202 3946 6944 5125 -1386 378 1484 A N ATOM 1450 CA ASP A 202 -53.548 11.579 58.091 1.00 44.55 A C ANISOU 1450 CA ASP A 202 4289 7330 5309 -1632 317 1642 A C ATOM 1451 C ASP A 202 -53.450 10.059 58.081 1.00 45.17 A C ANISOU 1451 C ASP A 202 4443 7293 5429 -1707 238 1822 A C ATOM 1452 O ASP A 202 -54.464 9.357 58.114 1.00 43.99 A O ANISOU 1452 O ASP A 202 4306 7184 5223 -1815 273 1756 A O ATOM 1453 CB ASP A 202 -54.544 12.091 59.128 1.00 47.65 A C ANISOU 1453 CB ASP A 202 4643 7948 5514 -1862 394 1478 A C ATOM 1454 CG ASP A 202 -54.105 11.807 60.556 1.00 48.58 A C ANISOU 1454 CG ASP A 202 4857 8118 5485 -2091 314 1597 A C ATOM 1455 OD1 ASP A 202 -53.557 10.714 60.809 1.00 48.36 A O ANISOU 1455 OD1 ASP A 202 4921 7981 5474 -2159 201 1807 A O ATOM 1456 OD2 ASP A 202 -54.304 12.682 61.431 1.00 49.24 A O1- ANISOU 1456 OD2 ASP A 202 4938 8327 5443 -2184 348 1464 A O1- ATOM 1457 N CYS A 203 -52.222 9.545 58.037 1.00 47.92 A N ANISOU 1457 N CYS A 203 4833 7487 5886 -1650 125 2042 A N ATOM 1458 CA CYS A 203 -52.001 8.115 57.868 1.00 47.30 A C ANISOU 1458 CA CYS A 203 4818 7257 5896 -1676 31 2214 A C ATOM 1459 C CYS A 203 -52.239 7.318 59.142 1.00 50.31 A C ANISOU 1459 C CYS A 203 5281 7709 6125 -1982 -56 2348 A C ATOM 1460 O CYS A 203 -52.089 6.092 59.121 1.00 51.39 A O ANISOU 1460 O CYS A 203 5486 7715 6324 -2028 -156 2497 A O ATOM 1461 CB CYS A 203 -50.581 7.862 57.354 1.00 49.75 A C ANISOU 1461 CB CYS A 203 5128 7366 6411 -1501 -65 2380 A C ATOM 1462 SG CYS A 203 -50.216 8.653 55.764 1.00 52.50 A S ANISOU 1462 SG CYS A 203 5411 7606 6930 -1169 40 2237 A S ATOM 1463 N ARG A 204 -52.597 7.976 60.243 1.00 52.87 A N ANISOU 1463 N ARG A 204 5631 8204 6253 -2151 -34 2245 A N ATOM 1464 CA ARG A 204 -53.034 7.280 61.447 1.00 57.38 A C ANISOU 1464 CA ARG A 204 6322 8832 6648 -2400 -106 2262 A C ATOM 1465 C ARG A 204 -54.530 6.987 61.422 1.00 60.59 A C ANISOU 1465 C ARG A 204 6727 9350 6943 -2512 17 2070 A C ATOM 1466 O ARG A 204 -54.947 5.836 61.581 1.00 61.17 A O ANISOU 1466 O ARG A 204 6884 9372 6986 -2626 -34 2132 A O ATOM 1467 CB ARG A 204 -52.691 8.113 62.682 1.00 58.44 A C ANISOU 1467 CB ARG A 204 6494 9088 6624 -2531 -139 2230 A C ATOM 1468 CG ARG A 204 -53.250 7.557 63.977 1.00 61.14 A C ANISOU 1468 CG ARG A 204 6962 9516 6753 -2807 -192 2212 A C ATOM 1469 CD ARG A 204 -53.561 8.685 64.940 1.00 61.99 A C ANISOU 1469 CD ARG A 204 7065 9808 6681 -2927 -117 2041 A C ATOM 1470 NE ARG A 204 -52.392 9.081 65.720 1.00 64.03 A N ANISOU 1470 NE ARG A 204 7368 10046 6913 -2963 -251 2181 A N ATOM 1471 CZ ARG A 204 -52.255 10.267 66.302 1.00 68.90 A C ANISOU 1471 CZ ARG A 204 7954 10785 7438 -2989 -199 2072 A C ATOM 1472 NH1 ARG A 204 -53.212 11.177 66.177 1.00 68.41 A N1+ ANISOU 1472 NH1 ARG A 204 7812 10864 7317 -2973 -21 1815 A N1+ ATOM 1473 NH2 ARG A 204 -51.159 10.547 66.995 1.00 71.09 A N ANISOU 1473 NH2 ARG A 204 8275 11036 7699 -3026 -333 2212 A N ATOM 1474 N SER A 205 -55.345 8.023 61.227 1.00 62.74 A N ANISOU 1474 N SER A 205 6900 9771 7167 -2479 172 1827 A N ATOM 1475 CA SER A 205 -56.795 7.903 61.214 1.00 63.63 A C ANISOU 1475 CA SER A 205 6983 9998 7196 -2573 296 1603 A C ATOM 1476 C SER A 205 -57.364 7.741 59.812 1.00 62.72 A C ANISOU 1476 C SER A 205 6763 9835 7231 -2403 378 1528 A C ATOM 1477 O SER A 205 -58.545 7.406 59.674 1.00 64.16 A O ANISOU 1477 O SER A 205 6919 10084 7376 -2473 462 1363 A O ATOM 1478 CB SER A 205 -57.434 9.126 61.885 1.00 64.42 A C ANISOU 1478 CB SER A 205 7024 10279 7172 -2639 404 1349 A C ATOM 1479 OG SER A 205 -57.133 10.312 61.169 1.00 63.65 A O ANISOU 1479 OG SER A 205 6806 10197 7182 -2436 460 1263 A O ATOM 1480 N LEU A 206 -56.559 7.973 58.776 1.00 60.17 A N ANISOU 1480 N LEU A 206 6390 9390 7082 -2171 351 1627 A N ATOM 1481 CA LEU A 206 -56.973 7.946 57.378 1.00 57.83 A C ANISOU 1481 CA LEU A 206 6047 8984 6942 -1913 396 1506 A C ATOM 1482 C LEU A 206 -57.926 9.080 57.028 1.00 53.90 A C ANISOU 1482 C LEU A 206 5441 8607 6432 -1831 510 1213 A C ATOM 1483 O LEU A 206 -58.565 9.042 55.969 1.00 53.23 A O ANISOU 1483 O LEU A 206 5321 8456 6447 -1664 545 1079 A O ATOM 1484 CB LEU A 206 -57.605 6.601 57.006 1.00 61.38 A C ANISOU 1484 CB LEU A 206 6546 9355 7420 -1964 384 1546 A C ATOM 1485 CG LEU A 206 -56.643 5.423 57.171 1.00 65.02 A C ANISOU 1485 CG LEU A 206 7112 9653 7940 -2004 248 1833 A C ATOM 1486 CD1 LEU A 206 -57.247 4.134 56.638 1.00 63.43 A C ANISOU 1486 CD1 LEU A 206 6957 9352 7791 -2018 236 1862 A C ATOM 1487 CD2 LEU A 206 -55.315 5.717 56.492 1.00 65.49 A C ANISOU 1487 CD2 LEU A 206 7166 9544 8172 -1761 182 1954 A C ATOM 1488 N GLU A 207 -58.053 10.081 57.896 1.00 51.02 A N ANISOU 1488 N GLU A 207 5021 8410 5953 -1948 558 1104 A N ATOM 1489 CA GLU A 207 -58.754 11.301 57.526 1.00 49.95 A C ANISOU 1489 CA GLU A 207 4775 8359 5846 -1833 639 831 A C ATOM 1490 C GLU A 207 -58.036 11.968 56.361 1.00 46.90 A C ANISOU 1490 C GLU A 207 4390 7818 5612 -1525 598 847 A C ATOM 1491 O GLU A 207 -56.804 11.976 56.292 1.00 45.95 A O ANISOU 1491 O GLU A 207 4327 7597 5534 -1450 533 1042 A O ATOM 1492 CB GLU A 207 -58.830 12.253 58.721 1.00 54.88 A C ANISOU 1492 CB GLU A 207 5345 9179 6328 -2017 693 730 A C ATOM 1493 CG GLU A 207 -59.303 13.659 58.377 1.00 61.27 A C ANISOU 1493 CG GLU A 207 6037 10051 7192 -1874 750 468 A C ATOM 1494 CD GLU A 207 -59.517 14.518 59.610 1.00 66.46 A C ANISOU 1494 CD GLU A 207 6690 10838 7723 -2016 788 324 A C ATOM 1495 OE1 GLU A 207 -59.628 13.950 60.717 1.00 68.44 A O ANISOU 1495 OE1 GLU A 207 7037 11135 7831 -2228 783 370 A O ATOM 1496 OE2 GLU A 207 -59.575 15.759 59.473 1.00 68.41 A O1- ANISOU 1496 OE2 GLU A 207 6854 11124 8014 -1906 813 161 A O1- ATOM 1497 N THR A 208 -58.812 12.524 55.435 1.00 45.24 A N ANISOU 1497 N THR A 208 4119 7582 5488 -1356 631 635 A N ATOM 1498 CA THR A 208 -58.257 13.124 54.231 1.00 42.02 A C ANISOU 1498 CA THR A 208 3737 7019 5209 -1083 592 636 A C ATOM 1499 C THR A 208 -58.897 14.477 53.972 1.00 39.23 A C ANISOU 1499 C THR A 208 3300 6727 4880 -983 615 383 A C ATOM 1500 O THR A 208 -60.086 14.677 54.238 1.00 34.39 A O ANISOU 1500 O THR A 208 2593 6225 4247 -1060 660 162 A O ATOM 1501 CB THR A 208 -58.458 12.223 53.014 1.00 41.72 A C ANISOU 1501 CB THR A 208 3756 6813 5281 -942 568 673 A C ATOM 1502 CG2 THR A 208 -57.795 10.880 53.247 1.00 41.39 A C ANISOU 1502 CG2 THR A 208 3792 6693 5242 -1029 533 918 A C ATOM 1503 OG1 THR A 208 -59.860 12.030 52.790 1.00 50.18 A O ANISOU 1503 OG1 THR A 208 4767 7942 6358 -973 604 467 A O ATOM 1504 N SER A 209 -58.093 15.402 53.451 1.00 37.16 A N ANISOU 1504 N SER A 209 3068 6382 4670 -815 579 409 A N ATOM 1505 CA SER A 209 -58.549 16.733 53.081 1.00 36.83 A C ANISOU 1505 CA SER A 209 2970 6356 4667 -694 570 193 A C ATOM 1506 C SER A 209 -58.065 17.061 51.678 1.00 36.75 A C ANISOU 1506 C SER A 209 3052 6151 4761 -455 512 225 A C ATOM 1507 O SER A 209 -56.872 16.929 51.384 1.00 37.53 A O ANISOU 1507 O SER A 209 3236 6150 4875 -394 497 415 A O ATOM 1508 CB SER A 209 -58.039 17.791 54.062 1.00 42.66 A C ANISOU 1508 CB SER A 209 3661 7217 5330 -772 587 174 A C ATOM 1509 OG SER A 209 -58.673 17.673 55.321 1.00 50.50 A O ANISOU 1509 OG SER A 209 4566 8403 6217 -1007 652 85 A O ATOM 1510 N LEU A 210 -58.986 17.481 50.815 1.00 36.16 A N ANISOU 1510 N LEU A 210 2963 6018 4760 -331 475 33 A N ATOM 1511 CA LEU A 210 -58.632 17.937 49.476 1.00 35.82 A C ANISOU 1511 CA LEU A 210 3026 5791 4793 -126 410 40 A C ATOM 1512 C LEU A 210 -58.296 19.419 49.579 1.00 35.08 A C ANISOU 1512 C LEU A 210 2924 5713 4694 -58 374 -46 A C ATOM 1513 O LEU A 210 -59.170 20.241 49.872 1.00 34.33 A O ANISOU 1513 O LEU A 210 2733 5694 4618 -60 349 -261 A O ATOM 1514 CB LEU A 210 -59.770 17.691 48.489 1.00 42.68 A C ANISOU 1514 CB LEU A 210 3903 6573 5739 -33 360 -114 A C ATOM 1515 CG LEU A 210 -60.220 16.246 48.268 1.00 46.30 A C ANISOU 1515 CG LEU A 210 4375 7007 6212 -89 390 -51 A C ATOM 1516 CD1 LEU A 210 -61.563 16.219 47.561 1.00 49.81 A C ANISOU 1516 CD1 LEU A 210 4784 7411 6730 -23 337 -260 A C ATOM 1517 CD2 LEU A 210 -59.188 15.478 47.467 1.00 45.12 A C ANISOU 1517 CD2 LEU A 210 4362 6699 6082 -18 396 166 A C ATOM 1518 N VAL A 211 -57.039 19.762 49.334 1.00 36.42 A N ANISOU 1518 N VAL A 211 3185 5805 4849 0 373 110 A N ATOM 1519 CA VAL A 211 -56.552 21.134 49.451 1.00 36.16 A C ANISOU 1519 CA VAL A 211 3159 5779 4800 55 342 59 A C ATOM 1520 C VAL A 211 -56.326 21.676 48.044 1.00 35.94 A C ANISOU 1520 C VAL A 211 3271 5561 4825 228 271 42 A C ATOM 1521 O VAL A 211 -55.502 21.125 47.301 1.00 34.33 A O ANISOU 1521 O VAL A 211 3181 5232 4630 277 292 195 A O ATOM 1522 CB VAL A 211 -55.265 21.221 50.285 1.00 33.83 A C ANISOU 1522 CB VAL A 211 2865 5546 4443 -27 392 240 A C ATOM 1523 CG1 VAL A 211 -54.813 22.671 50.382 1.00 36.48 A C ANISOU 1523 CG1 VAL A 211 3209 5889 4761 29 362 176 A C ATOM 1524 CG2 VAL A 211 -55.481 20.630 51.666 1.00 29.58 A C ANISOU 1524 CG2 VAL A 211 2219 5186 3833 -223 447 273 A C ATOM 1525 N PRO A 212 -57.032 22.727 47.633 1.00 36.50 A N ANISOU 1525 N PRO A 212 3342 5593 4932 316 183 -146 A N ATOM 1526 CA PRO A 212 -56.903 23.201 46.250 1.00 35.73 A C ANISOU 1526 CA PRO A 212 3408 5300 4868 460 95 -160 A C ATOM 1527 C PRO A 212 -55.477 23.611 45.915 1.00 39.09 A C ANISOU 1527 C PRO A 212 3959 5647 5247 488 126 1 A C ATOM 1528 O PRO A 212 -54.793 24.275 46.698 1.00 43.01 A O ANISOU 1528 O PRO A 212 4410 6228 5703 444 158 38 A O ATOM 1529 CB PRO A 212 -57.858 24.399 46.190 1.00 34.05 A C ANISOU 1529 CB PRO A 212 3150 5082 4707 526 -25 -392 A C ATOM 1530 CG PRO A 212 -58.825 24.195 47.304 1.00 29.78 A C ANISOU 1530 CG PRO A 212 2405 4721 4189 426 13 -537 A C ATOM 1531 CD PRO A 212 -58.144 23.371 48.356 1.00 38.13 A C ANISOU 1531 CD PRO A 212 3399 5924 5166 277 151 -373 A C ATOM 1532 N LEU A 213 -55.035 23.196 44.727 1.00 40.63 A N ANISOU 1532 N LEU A 213 4312 5676 5448 553 124 86 A N ATOM 1533 CA LEU A 213 -53.749 23.585 44.145 1.00 43.57 A C ANISOU 1533 CA LEU A 213 4824 5946 5786 582 158 207 A C ATOM 1534 C LEU A 213 -54.044 23.953 42.694 1.00 49.58 A C ANISOU 1534 C LEU A 213 5776 6517 6546 672 69 143 A C ATOM 1535 O LEU A 213 -53.891 23.134 41.787 1.00 56.31 A O ANISOU 1535 O LEU A 213 6734 7257 7404 686 102 206 A O ATOM 1536 CB LEU A 213 -52.709 22.470 44.255 1.00 39.97 A C ANISOU 1536 CB LEU A 213 4362 5487 5338 529 280 394 A C ATOM 1537 CG LEU A 213 -51.474 22.767 45.106 1.00 39.78 A C ANISOU 1537 CG LEU A 213 4281 5541 5292 471 350 514 A C ATOM 1538 CD1 LEU A 213 -50.471 21.626 44.978 1.00 36.92 A C ANISOU 1538 CD1 LEU A 213 3923 5129 4977 442 444 682 A C ATOM 1539 CD2 LEU A 213 -50.846 24.093 44.697 1.00 39.96 A C ANISOU 1539 CD2 LEU A 213 4408 5501 5274 517 322 484 A C ATOM 1540 N SER A 214 -54.474 25.199 42.479 1.00 55.50 A N ANISOU 1540 N SER A 214 6578 7224 7287 727 -54 17 A N ATOM 1541 CA SER A 214 -54.948 25.662 41.178 1.00 58.05 A C ANISOU 1541 CA SER A 214 7090 7360 7605 803 -186 -60 A C ATOM 1542 C SER A 214 -54.630 27.153 41.049 1.00 59.22 A C ANISOU 1542 C SER A 214 7335 7451 7717 836 -284 -113 A C ATOM 1543 O SER A 214 -55.487 28.030 41.153 1.00 62.21 A O ANISOU 1543 O SER A 214 7684 7815 8138 887 -433 -266 A O ATOM 1544 CB SER A 214 -56.445 25.399 40.998 1.00 62.20 A C ANISOU 1544 CB SER A 214 7555 7874 8206 848 -305 -216 A C ATOM 1545 OG SER A 214 -57.185 25.922 42.088 1.00 65.78 A O ANISOU 1545 OG SER A 214 7809 8471 8715 841 -346 -355 A O ATOM 1546 N ASP A 215 -53.360 27.454 40.811 1.00 54.53 A N ANISOU 1546 N ASP A 215 6853 6814 7051 803 -201 8 A N ATOM 1547 CA ASP A 215 -52.901 28.833 40.662 1.00 51.98 A C ANISOU 1547 CA ASP A 215 6642 6431 6678 818 -278 -21 A C ATOM 1548 C ASP A 215 -52.073 28.955 39.392 1.00 49.51 A C ANISOU 1548 C ASP A 215 6591 5941 6279 799 -258 61 A C ATOM 1549 O ASP A 215 -50.943 28.426 39.341 1.00 49.19 A O ANISOU 1549 O ASP A 215 6568 5916 6207 741 -92 187 A O ATOM 1550 CB ASP A 215 -52.093 29.271 41.880 1.00 48.16 A C ANISOU 1550 CB ASP A 215 6012 6105 6182 770 -181 30 A C ATOM 1551 CG ASP A 215 -51.860 30.769 41.915 1.00 46.75 A C ANISOU 1551 CG ASP A 215 5911 5886 5967 790 -280 -31 A C ATOM 1552 OD1 ASP A 215 -52.135 31.443 40.899 1.00 47.47 A O ANISOU 1552 OD1 ASP A 215 6201 5806 6030 832 -418 -86 A O ATOM 1553 OD2 ASP A 215 -51.414 31.275 42.965 1.00 45.40 A O1- ANISOU 1553 OD2 ASP A 215 5611 5848 5792 758 -229 -22 A O1- ATOM 1554 N PRO A 216 -52.576 29.629 38.356 1.00 50.59 A N ANISOU 1554 N PRO A 216 6938 5905 6380 834 -424 -12 A N ATOM 1555 CA PRO A 216 -51.765 29.813 37.141 1.00 49.53 A C ANISOU 1555 CA PRO A 216 7080 5602 6136 782 -399 59 A C ATOM 1556 C PRO A 216 -50.407 30.446 37.407 1.00 47.37 A C ANISOU 1556 C PRO A 216 6844 5360 5794 719 -279 142 A C ATOM 1557 O PRO A 216 -49.496 30.290 36.584 1.00 49.92 A O ANISOU 1557 O PRO A 216 7342 5589 6036 648 -174 215 A O ATOM 1558 CB PRO A 216 -52.641 30.719 36.262 1.00 47.58 A C ANISOU 1558 CB PRO A 216 7038 5177 5863 826 -649 -46 A C ATOM 1559 CG PRO A 216 -53.696 31.268 37.165 1.00 48.68 A C ANISOU 1559 CG PRO A 216 6980 5401 6116 911 -798 -180 A C ATOM 1560 CD PRO A 216 -53.907 30.242 38.232 1.00 50.24 A C ANISOU 1560 CD PRO A 216 6890 5799 6398 912 -650 -170 A C ATOM 1561 N LYS A 217 -50.247 31.174 38.515 1.00 47.09 A N ANISOU 1561 N LYS A 217 6651 5452 5788 734 -286 121 A N ATOM 1562 CA LYS A 217 -48.957 31.742 38.889 1.00 51.34 A C ANISOU 1562 CA LYS A 217 7197 6038 6273 675 -170 199 A C ATOM 1563 C LYS A 217 -48.018 30.720 39.514 1.00 47.81 A C ANISOU 1563 C LYS A 217 6583 5717 5866 627 46 314 A C ATOM 1564 O LYS A 217 -46.820 30.995 39.637 1.00 44.94 A O ANISOU 1564 O LYS A 217 6237 5371 5469 571 162 387 A O ATOM 1565 CB LYS A 217 -49.156 32.913 39.857 1.00 55.35 A C ANISOU 1565 CB LYS A 217 7598 6633 6800 706 -266 129 A C ATOM 1566 CG LYS A 217 -50.146 33.955 39.363 1.00 60.51 A C ANISOU 1566 CG LYS A 217 8382 7156 7452 767 -509 -1 A C ATOM 1567 CD LYS A 217 -49.677 34.559 38.046 1.00 65.34 A C ANISOU 1567 CD LYS A 217 9322 7558 7946 721 -575 29 A C ATOM 1568 CE LYS A 217 -50.688 35.546 37.486 1.00 70.25 A C ANISOU 1568 CE LYS A 217 10097 8019 8576 782 -855 -90 A C ATOM 1569 NZ LYS A 217 -51.914 34.865 36.967 1.00 71.84 A N1+ ANISOU 1569 NZ LYS A 217 10299 8149 8847 844 -980 -163 A N1+ ATOM 1570 N LEU A 218 -48.525 29.552 39.892 1.00 44.59 A N ANISOU 1570 N LEU A 218 6020 5387 5535 646 92 331 A N ATOM 1571 CA LEU A 218 -47.752 28.540 40.597 1.00 41.85 A C ANISOU 1571 CA LEU A 218 5502 5153 5246 606 258 440 A C ATOM 1572 C LEU A 218 -47.551 27.330 39.698 1.00 43.73 A C ANISOU 1572 C LEU A 218 5811 5297 5508 590 352 492 A C ATOM 1573 O LEU A 218 -48.498 26.861 39.055 1.00 48.52 A O ANISOU 1573 O LEU A 218 6485 5831 6118 622 282 439 A O ATOM 1574 CB LEU A 218 -48.457 28.129 41.892 1.00 40.69 A C ANISOU 1574 CB LEU A 218 5115 5180 5167 618 236 425 A C ATOM 1575 CG LEU A 218 -47.768 27.127 42.819 1.00 40.33 A C ANISOU 1575 CG LEU A 218 4888 5256 5180 567 365 545 A C ATOM 1576 CD1 LEU A 218 -46.418 27.649 43.296 1.00 37.84 A C ANISOU 1576 CD1 LEU A 218 4544 4981 4851 522 448 628 A C ATOM 1577 CD2 LEU A 218 -48.670 26.800 44.000 1.00 39.11 A C ANISOU 1577 CD2 LEU A 218 4540 5261 5059 554 324 509 A C ATOM 1578 N ALA A 219 -46.320 26.831 39.657 1.00 41.70 A N ANISOU 1578 N ALA A 219 5531 5036 5277 540 509 585 A N ATOM 1579 CA ALA A 219 -45.975 25.639 38.902 1.00 38.60 A C ANISOU 1579 CA ALA A 219 5175 4560 4931 519 622 627 A C ATOM 1580 C ALA A 219 -45.303 24.628 39.820 1.00 41.21 A C ANISOU 1580 C ALA A 219 5287 4992 5380 504 729 727 A C ATOM 1581 O ALA A 219 -44.623 24.994 40.783 1.00 44.54 A O ANISOU 1581 O ALA A 219 5582 5515 5827 484 754 779 A O ATOM 1582 CB ALA A 219 -45.051 25.977 37.725 1.00 33.40 A C ANISOU 1582 CB ALA A 219 4725 3758 4207 460 715 618 A C ATOM 1583 N VAL A 220 -45.500 23.351 39.511 1.00 37.28 A N ANISOU 1583 N VAL A 220 4753 4457 4956 509 780 755 A N ATOM 1584 CA VAL A 220 -44.846 22.251 40.210 1.00 38.24 A C ANISOU 1584 CA VAL A 220 4692 4632 5205 493 865 854 A C ATOM 1585 C VAL A 220 -43.919 21.576 39.211 1.00 41.41 A C ANISOU 1585 C VAL A 220 5163 4901 5672 469 1006 862 A C ATOM 1586 O VAL A 220 -44.378 20.937 38.256 1.00 42.73 A O ANISOU 1586 O VAL A 220 5434 4967 5834 475 1027 822 A O ATOM 1587 CB VAL A 220 -45.859 21.257 40.792 1.00 30.77 A C ANISOU 1587 CB VAL A 220 3628 3755 4308 512 804 876 A C ATOM 1588 CG1 VAL A 220 -45.142 20.035 41.356 1.00 28.05 A C ANISOU 1588 CG1 VAL A 220 3129 3428 4100 489 875 987 A C ATOM 1589 CG2 VAL A 220 -46.713 21.932 41.860 1.00 31.21 A C ANISOU 1589 CG2 VAL A 220 3594 3956 4307 515 690 846 A C ATOM 1590 N LEU A 221 -42.615 21.709 39.430 1.00 37.09 A N ANISOU 1590 N LEU A 221 4550 4352 5191 436 1105 903 A N ATOM 1591 CA LEU A 221 -41.614 21.170 38.522 1.00 37.67 A C ANISOU 1591 CA LEU A 221 4667 4303 5343 401 1259 883 A C ATOM 1592 C LEU A 221 -41.055 19.884 39.112 1.00 41.72 A C ANISOU 1592 C LEU A 221 4975 4826 6052 414 1306 963 A C ATOM 1593 O LEU A 221 -40.456 19.899 40.193 1.00 41.61 A O ANISOU 1593 O LEU A 221 4795 4896 6121 413 1281 1042 A O ATOM 1594 CB LEU A 221 -40.490 22.177 38.278 1.00 37.97 A C ANISOU 1594 CB LEU A 221 4766 4318 5345 348 1345 852 A C ATOM 1595 CG LEU A 221 -39.426 21.746 37.267 1.00 37.95 A C ANISOU 1595 CG LEU A 221 4814 4190 5415 290 1529 796 A C ATOM 1596 CD1 LEU A 221 -40.073 21.469 35.917 1.00 39.57 A C ANISOU 1596 CD1 LEU A 221 5237 4273 5525 262 1561 714 A C ATOM 1597 CD2 LEU A 221 -38.344 22.801 37.131 1.00 35.71 A C ANISOU 1597 CD2 LEU A 221 4580 3899 5088 224 1615 758 A C ATOM 1598 N ILE A 222 -41.246 18.780 38.402 1.00 42.02 A N ANISOU 1598 N ILE A 222 5032 4768 6164 422 1362 943 A N ATOM 1599 CA ILE A 222 -40.724 17.483 38.805 1.00 38.69 A C ANISOU 1599 CA ILE A 222 4434 4321 5947 436 1398 1009 A C ATOM 1600 C ILE A 222 -39.501 17.191 37.951 1.00 40.22 A C ANISOU 1600 C ILE A 222 4629 4390 6261 404 1570 942 A C ATOM 1601 O ILE A 222 -39.569 17.261 36.717 1.00 41.06 A O ANISOU 1601 O ILE A 222 4906 4397 6298 369 1669 841 A O ATOM 1602 CB ILE A 222 -41.790 16.387 38.647 1.00 37.80 A C ANISOU 1602 CB ILE A 222 4324 4184 5852 466 1344 1024 A C ATOM 1603 CG1 ILE A 222 -43.048 16.761 39.431 1.00 41.62 A C ANISOU 1603 CG1 ILE A 222 4808 4796 6211 483 1191 1056 A C ATOM 1604 CG2 ILE A 222 -41.252 15.046 39.120 1.00 35.34 A C ANISOU 1604 CG2 ILE A 222 3835 3835 5758 479 1358 1101 A C ATOM 1605 CD1 ILE A 222 -44.164 15.765 39.284 1.00 41.88 A C ANISOU 1605 CD1 ILE A 222 4847 4816 6249 503 1138 1060 A C ATOM 1606 N THR A 223 -38.383 16.868 38.596 1.00 42.79 A N ANISOU 1606 N THR A 223 4770 4717 6773 405 1604 989 A N ATOM 1607 CA THR A 223 -37.130 16.601 37.898 1.00 45.46 A C ANISOU 1607 CA THR A 223 5065 4942 7264 373 1774 905 A C ATOM 1608 C THR A 223 -36.688 15.175 38.186 1.00 48.14 A C ANISOU 1608 C THR A 223 5213 5210 7869 412 1776 945 A C ATOM 1609 O THR A 223 -36.414 14.826 39.339 1.00 49.07 A O ANISOU 1609 O THR A 223 5154 5379 8112 443 1662 1059 A O ATOM 1610 CB THR A 223 -36.037 17.590 38.311 1.00 46.73 A C ANISOU 1610 CB THR A 223 5166 5147 7441 340 1816 897 A C ATOM 1611 CG2 THR A 223 -34.734 17.275 37.588 1.00 50.31 A C ANISOU 1611 CG2 THR A 223 5556 5486 8075 298 2006 785 A C ATOM 1612 OG1 THR A 223 -36.447 18.924 37.987 1.00 46.55 A O ANISOU 1612 OG1 THR A 223 5338 5175 7174 301 1807 856 A O ATOM 1613 N ASN A 224 -36.616 14.358 37.138 1.00 49.95 A N ANISOU 1613 N ASN A 224 5484 5313 8181 402 1898 850 A N ATOM 1614 CA ASN A 224 -36.165 12.978 37.253 1.00 51.04 A C ANISOU 1614 CA ASN A 224 5447 5355 8592 440 1910 864 A C ATOM 1615 C ASN A 224 -34.653 12.938 37.066 1.00 55.52 A C ANISOU 1615 C ASN A 224 5869 5840 9387 420 2047 773 A C ATOM 1616 O ASN A 224 -34.144 13.303 36.000 1.00 58.32 A O ANISOU 1616 O ASN A 224 6318 6130 9712 355 2236 620 A O ATOM 1617 CB ASN A 224 -36.868 12.101 36.216 1.00 52.82 A C ANISOU 1617 CB ASN A 224 5782 5483 8803 438 1977 792 A C ATOM 1618 CG ASN A 224 -36.563 10.625 36.391 1.00 54.26 A C ANISOU 1618 CG ASN A 224 5789 5563 9266 485 1961 815 A C ATOM 1619 ND2 ASN A 224 -37.372 9.776 35.763 1.00 53.24 A N ANISOU 1619 ND2 ASN A 224 5740 5371 9117 495 1972 791 A N ATOM 1620 OD1 ASN A 224 -35.610 10.251 37.076 1.00 55.89 A O ANISOU 1620 OD1 ASN A 224 5789 5736 9709 513 1929 853 A O ATOM 1621 N SER A 225 -33.938 12.500 38.104 1.00 54.92 A N ANISOU 1621 N SER A 225 5565 5763 9538 463 1947 862 A N ATOM 1622 CA SER A 225 -32.491 12.342 38.022 1.00 55.30 A C ANISOU 1622 CA SER A 225 5433 5722 9856 458 2052 771 A C ATOM 1623 C SER A 225 -32.077 11.189 37.120 1.00 57.68 A C ANISOU 1623 C SER A 225 5661 5859 10395 466 2188 637 A C ATOM 1624 O SER A 225 -30.899 11.101 36.757 1.00 60.73 A O ANISOU 1624 O SER A 225 5915 6158 11003 446 2327 502 A O ATOM 1625 CB SER A 225 -31.902 12.144 39.420 1.00 55.90 A C ANISOU 1625 CB SER A 225 5291 5830 10120 505 1869 913 A C ATOM 1626 OG SER A 225 -32.314 10.910 39.978 1.00 57.14 A O ANISOU 1626 OG SER A 225 5351 5933 10426 560 1713 1026 A O ATOM 1627 N ASN A 226 -33.012 10.317 36.745 1.00 60.95 A N ANISOU 1627 N ASN A 226 6153 6229 10775 489 2157 658 A N ATOM 1628 CA ASN A 226 -32.706 9.115 35.973 1.00 64.23 A C ANISOU 1628 CA ASN A 226 6491 6486 11428 503 2266 541 A C ATOM 1629 C ASN A 226 -31.666 8.256 36.692 1.00 66.36 A C ANISOU 1629 C ASN A 226 6471 6655 12089 568 2186 562 A C ATOM 1630 O ASN A 226 -30.634 7.882 36.133 1.00 66.76 A O ANISOU 1630 O ASN A 226 6409 6587 12368 547 2315 397 A O ATOM 1631 CB ASN A 226 -32.245 9.470 34.557 1.00 64.86 A C ANISOU 1631 CB ASN A 226 6687 6499 11459 413 2541 315 A C ATOM 1632 CG ASN A 226 -33.358 10.065 33.714 1.00 67.24 A C ANISOU 1632 CG ASN A 226 7293 6856 11399 348 2593 295 A C ATOM 1633 ND2 ASN A 226 -33.242 11.354 33.401 1.00 68.73 A N ANISOU 1633 ND2 ASN A 226 7638 7117 11358 270 2668 250 A N ATOM 1634 OD1 ASN A 226 -34.310 9.373 33.344 1.00 65.96 A O ANISOU 1634 OD1 ASN A 226 7227 6663 11171 367 2555 319 A O ATOM 1635 N VAL A 227 -31.954 7.948 37.954 1.00 69.95 A N ANISOU 1635 N VAL A 227 6834 7157 12588 623 1939 763 A N ATOM 1636 CA VAL A 227 -31.149 7.016 38.734 1.00 76.33 A C ANISOU 1636 CA VAL A 227 7403 7856 13743 680 1790 821 A C ATOM 1637 C VAL A 227 -32.074 6.064 39.480 1.00 79.33 A C ANISOU 1637 C VAL A 227 7780 8230 14134 725 1571 1009 A C ATOM 1638 O VAL A 227 -33.216 6.410 39.781 1.00 79.30 A O ANISOU 1638 O VAL A 227 7942 8356 13833 699 1494 1123 A O ATOM 1639 CB VAL A 227 -30.213 7.747 39.714 1.00 79.93 A C ANISOU 1639 CB VAL A 227 7748 8371 14252 667 1679 882 A C ATOM 1640 CG1 VAL A 227 -29.539 6.749 40.645 1.00 82.17 A C ANISOU 1640 CG1 VAL A 227 7858 8549 14814 695 1446 970 A C ATOM 1641 CG2 VAL A 227 -29.168 8.542 38.953 1.00 80.97 A C ANISOU 1641 CG2 VAL A 227 7884 8488 14393 608 1885 677 A C ATOM 1642 N SER A 234 -33.162 -2.717 48.721 1.00 73.49 A N ANISOU 1642 N SER A 234 6779 7003 14140 405 -871 2524 A N ATOM 1643 CA SER A 234 -32.898 -1.324 49.061 1.00 73.26 A C ANISOU 1643 CA SER A 234 6746 7115 13973 400 -802 2544 A C ATOM 1644 C SER A 234 -32.696 -1.126 50.560 1.00 75.10 A C ANISOU 1644 C SER A 234 7009 7408 14118 281 -1063 2739 A C ATOM 1645 O SER A 234 -32.615 -2.086 51.327 1.00 77.80 A O ANISOU 1645 O SER A 234 7367 7663 14530 202 -1306 2848 A O ATOM 1646 CB SER A 234 -34.039 -0.428 48.573 1.00 73.17 A C ANISOU 1646 CB SER A 234 6854 7278 13669 416 -596 2540 A C ATOM 1647 OG SER A 234 -34.025 -0.305 47.162 1.00 73.00 A O ANISOU 1647 OG SER A 234 6807 7211 13720 521 -332 2340 A O ATOM 1648 N GLU A 235 -32.620 0.139 50.966 1.00 71.81 A N ANISOU 1648 N GLU A 235 6606 7141 13536 261 -1012 2778 A N ATOM 1649 CA GLU A 235 -32.449 0.520 52.360 1.00 71.74 A C ANISOU 1649 CA GLU A 235 6636 7215 13405 137 -1230 2952 A C ATOM 1650 C GLU A 235 -33.765 0.878 53.040 1.00 68.89 A C ANISOU 1650 C GLU A 235 6443 7050 12682 18 -1260 3103 A C ATOM 1651 O GLU A 235 -33.801 0.999 54.270 1.00 69.29 A O ANISOU 1651 O GLU A 235 6557 7175 12594 -123 -1454 3254 A O ATOM 1652 CB GLU A 235 -31.473 1.698 52.463 1.00 71.99 A C ANISOU 1652 CB GLU A 235 6576 7294 13484 176 -1164 2897 A C ATOM 1653 CG GLU A 235 -30.723 1.778 53.777 1.00 75.47 A C ANISOU 1653 CG GLU A 235 6998 7722 13956 70 -1421 3028 A C ATOM 1654 CD GLU A 235 -29.438 0.967 53.764 1.00 78.76 A C ANISOU 1654 CD GLU A 235 7277 7911 14735 110 -1557 2957 A C ATOM 1655 OE1 GLU A 235 -28.705 1.025 52.753 1.00 79.50 A O ANISOU 1655 OE1 GLU A 235 7247 7906 15054 232 -1387 2766 A O ATOM 1656 OE2 GLU A 235 -29.158 0.279 54.767 1.00 79.70 A O1- ANISOU 1656 OE2 GLU A 235 7418 7951 14913 9 -1833 3085 A O1- ATOM 1657 N TYR A 236 -34.834 1.058 52.264 1.00 64.52 A N ANISOU 1657 N TYR A 236 5965 6579 11969 60 -1068 3053 A N ATOM 1658 CA TYR A 236 -36.160 1.382 52.792 1.00 60.84 A C ANISOU 1658 CA TYR A 236 5658 6297 11163 -55 -1068 3166 A C ATOM 1659 C TYR A 236 -36.616 0.486 53.936 1.00 61.21 A C ANISOU 1659 C TYR A 236 5806 6351 11099 -233 -1312 3322 A C ATOM 1660 O TYR A 236 -36.994 1.019 54.992 1.00 60.11 A O ANISOU 1660 O TYR A 236 5756 6369 10715 -383 -1400 3435 A O ATOM 1661 CB TYR A 236 -37.167 1.308 51.635 1.00 58.62 A C ANISOU 1661 CB TYR A 236 5433 6031 10807 27 -850 3067 A C ATOM 1662 CG TYR A 236 -38.573 1.768 51.963 1.00 58.14 A C ANISOU 1662 CG TYR A 236 5528 6181 10382 -88 -787 3106 A C ATOM 1663 CD1 TYR A 236 -39.450 0.954 52.673 1.00 59.29 A C ANISOU 1663 CD1 TYR A 236 5783 6348 10396 -235 -928 3241 A C ATOM 1664 CD2 TYR A 236 -39.038 3.003 51.525 1.00 56.59 A C ANISOU 1664 CD2 TYR A 236 5370 6169 9962 -63 -576 2965 A C ATOM 1665 CE1 TYR A 236 -40.736 1.370 52.964 1.00 56.99 A C ANISOU 1665 CE1 TYR A 236 5617 6267 9769 -355 -847 3221 A C ATOM 1666 CE2 TYR A 236 -40.326 3.424 51.809 1.00 56.88 A C ANISOU 1666 CE2 TYR A 236 5530 6405 9678 -168 -514 2949 A C ATOM 1667 CZ TYR A 236 -41.170 2.601 52.527 1.00 57.41 A C ANISOU 1667 CZ TYR A 236 5686 6499 9629 -314 -641 3069 A C ATOM 1668 OH TYR A 236 -42.456 3.002 52.820 1.00 56.24 A O ANISOU 1668 OH TYR A 236 5641 6550 9180 -427 -569 3029 A O ATOM 1669 N PRO A 237 -36.618 -0.842 53.809 1.00 63.19 A N ANISOU 1669 N PRO A 237 6059 6448 11502 -237 -1424 3327 A N ATOM 1670 CA PRO A 237 -37.060 -1.684 54.935 1.00 64.42 A C ANISOU 1670 CA PRO A 237 6330 6612 11533 -420 -1663 3476 A C ATOM 1671 C PRO A 237 -36.230 -1.508 56.193 1.00 68.77 A C ANISOU 1671 C PRO A 237 6873 7164 12092 -538 -1895 3588 A C ATOM 1672 O PRO A 237 -36.726 -1.801 57.288 1.00 71.82 A O ANISOU 1672 O PRO A 237 7389 7627 12273 -729 -2064 3716 A O ATOM 1673 CB PRO A 237 -36.941 -3.110 54.376 1.00 64.33 A C ANISOU 1673 CB PRO A 237 6287 6398 11759 -361 -1732 3435 A C ATOM 1674 CG PRO A 237 -35.965 -2.997 53.243 1.00 64.01 A C ANISOU 1674 CG PRO A 237 6077 6218 12027 -164 -1588 3269 A C ATOM 1675 CD PRO A 237 -36.181 -1.639 52.653 1.00 62.97 A C ANISOU 1675 CD PRO A 237 5932 6230 11764 -86 -1339 3189 A C ATOM 1676 N VAL A 238 -34.989 -1.032 56.077 1.00 69.19 A N ANISOU 1676 N VAL A 238 6786 7136 12367 -443 -1903 3535 A N ATOM 1677 CA VAL A 238 -34.173 -0.801 57.264 1.00 70.41 A C ANISOU 1677 CA VAL A 238 6934 7288 12533 -555 -2123 3638 A C ATOM 1678 C VAL A 238 -34.677 0.418 58.028 1.00 70.60 A C ANISOU 1678 C VAL A 238 7049 7551 12226 -675 -2078 3710 A C ATOM 1679 O VAL A 238 -34.726 0.415 59.265 1.00 72.86 A O ANISOU 1679 O VAL A 238 7430 7905 12349 -860 -2268 3834 A O ATOM 1680 CB VAL A 238 -32.691 -0.654 56.872 1.00 67.47 A C ANISOU 1680 CB VAL A 238 6378 6752 12506 -419 -2133 3541 A C ATOM 1681 CG1 VAL A 238 -31.844 -0.353 58.097 1.00 64.19 A C ANISOU 1681 CG1 VAL A 238 5959 6328 12102 -535 -2361 3648 A C ATOM 1682 CG2 VAL A 238 -32.201 -1.912 56.175 1.00 67.31 A C ANISOU 1682 CG2 VAL A 238 6266 6496 12811 -320 -2183 3455 A C ATOM 1683 N ARG A 239 -35.049 1.481 57.308 1.00 66.62 A N ANISOU 1683 N ARG A 239 6520 7176 11617 -578 -1826 3624 A N ATOM 1684 CA ARG A 239 -35.596 2.669 57.959 1.00 66.01 A C ANISOU 1684 CA ARG A 239 6524 7332 11223 -687 -1764 3674 A C ATOM 1685 C ARG A 239 -36.885 2.355 58.710 1.00 68.41 A C ANISOU 1685 C ARG A 239 7006 7784 11202 -887 -1812 3754 A C ATOM 1686 O ARG A 239 -37.069 2.803 59.848 1.00 69.87 A O ANISOU 1686 O ARG A 239 7279 8112 11156 -1068 -1908 3833 A O ATOM 1687 CB ARG A 239 -35.840 3.765 56.923 1.00 61.20 A C ANISOU 1687 CB ARG A 239 5864 6814 10573 -537 -1483 3557 A C ATOM 1688 CG ARG A 239 -34.596 4.219 56.183 1.00 56.84 A C ANISOU 1688 CG ARG A 239 5145 6145 10306 -356 -1402 3451 A C ATOM 1689 CD ARG A 239 -33.563 4.816 57.128 1.00 54.65 A C ANISOU 1689 CD ARG A 239 4815 5885 10066 -419 -1545 3512 A C ATOM 1690 NE ARG A 239 -32.395 5.331 56.414 1.00 52.79 A N ANISOU 1690 NE ARG A 239 4421 5553 10085 -259 -1441 3387 A N ATOM 1691 CZ ARG A 239 -31.365 4.583 56.030 1.00 55.38 A C ANISOU 1691 CZ ARG A 239 4630 5669 10743 -175 -1500 3311 A C ATOM 1692 NH1 ARG A 239 -31.352 3.284 56.298 1.00 51.66 A N1+ ANISOU 1692 NH1 ARG A 239 4178 5052 10397 -225 -1679 3362 A N1+ ATOM 1693 NH2 ARG A 239 -30.345 5.133 55.382 1.00 55.35 A N ANISOU 1693 NH2 ARG A 239 4492 5599 10941 -51 -1376 3172 A N ATOM 1694 N ARG A 240 -37.792 1.591 58.091 1.00 70.97 A N ANISOU 1694 N ARG A 240 7386 8080 11499 -867 -1738 3719 A N ATOM 1695 CA ARG A 240 -39.025 1.212 58.777 1.00 75.50 A C ANISOU 1695 CA ARG A 240 8125 8787 11775 -1065 -1774 3774 A C ATOM 1696 C ARG A 240 -38.731 0.429 60.048 1.00 81.04 A C ANISOU 1696 C ARG A 240 8909 9443 12441 -1257 -2055 3899 A C ATOM 1697 O ARG A 240 -39.386 0.632 61.077 1.00 85.77 A O ANISOU 1697 O ARG A 240 9640 10204 12744 -1470 -2109 3951 A O ATOM 1698 CB ARG A 240 -39.927 0.386 57.856 1.00 77.16 A C ANISOU 1698 CB ARG A 240 8370 8940 12008 -1003 -1665 3716 A C ATOM 1699 CG ARG A 240 -41.357 0.232 58.389 1.00 76.26 A C ANISOU 1699 CG ARG A 240 8415 9000 11562 -1198 -1629 3730 A C ATOM 1700 CD ARG A 240 -42.298 -0.393 57.364 1.00 75.01 A C ANISOU 1700 CD ARG A 240 8280 8801 11420 -1125 -1487 3657 A C ATOM 1701 NE ARG A 240 -43.704 -0.307 57.764 1.00 78.60 A N ANISOU 1701 NE ARG A 240 8862 9446 11555 -1301 -1403 3633 A N ATOM 1702 CZ ARG A 240 -44.728 -0.621 56.975 1.00 81.38 A C ANISOU 1702 CZ ARG A 240 9244 9818 11860 -1271 -1253 3557 A C ATOM 1703 NH1 ARG A 240 -44.509 -1.038 55.736 1.00 82.14 A N1+ ANISOU 1703 NH1 ARG A 240 9265 9751 12195 -1071 -1172 3506 A N1+ ATOM 1704 NH2 ARG A 240 -45.975 -0.502 57.414 1.00 82.74 A N ANISOU 1704 NH2 ARG A 240 9515 10173 11749 -1445 -1177 3516 A N ATOM 1705 N ARG A 241 -37.743 -0.467 60.002 1.00 79.58 A N ANISOU 1705 N ARG A 241 8650 9034 12554 -1192 -2236 3935 A N ATOM 1706 CA ARG A 241 -37.410 -1.249 61.187 1.00 79.52 A C ANISOU 1706 CA ARG A 241 8725 8957 12531 -1375 -2526 4058 A C ATOM 1707 C ARG A 241 -36.879 -0.355 62.301 1.00 77.55 A C ANISOU 1707 C ARG A 241 8499 8816 12149 -1507 -2628 4124 A C ATOM 1708 O ARG A 241 -37.275 -0.500 63.463 1.00 79.36 A O ANISOU 1708 O ARG A 241 8874 9139 12141 -1739 -2771 4211 A O ATOM 1709 CB ARG A 241 -36.396 -2.339 60.831 1.00 84.26 A C ANISOU 1709 CB ARG A 241 9223 9283 13512 -1263 -2695 4062 A C ATOM 1710 CG ARG A 241 -36.957 -3.428 59.927 1.00 87.48 A C ANISOU 1710 CG ARG A 241 9633 9574 14031 -1175 -2639 4010 A C ATOM 1711 CD ARG A 241 -36.086 -4.676 59.926 1.00 91.70 A C ANISOU 1711 CD ARG A 241 10104 9849 14888 -1136 -2867 4034 A C ATOM 1712 NE ARG A 241 -34.876 -4.515 59.126 1.00 92.65 A N ANISOU 1712 NE ARG A 241 10022 9810 15369 -927 -2816 3927 A N ATOM 1713 CZ ARG A 241 -34.789 -4.824 57.835 1.00 91.19 A C ANISOU 1713 CZ ARG A 241 9726 9523 15400 -734 -2644 3790 A C ATOM 1714 NH1 ARG A 241 -35.845 -5.309 57.195 1.00 87.70 A N1+ ANISOU 1714 NH1 ARG A 241 9355 9113 14855 -715 -2516 3757 A N1+ ATOM 1715 NH2 ARG A 241 -33.646 -4.650 57.185 1.00 91.88 A N ANISOU 1715 NH2 ARG A 241 9633 9474 15802 -571 -2593 3675 A N ATOM 1716 N GLN A 242 -35.997 0.585 61.961 1.00 74.48 A N ANISOU 1716 N GLN A 242 7974 8421 11903 -1370 -2549 4076 A N ATOM 1717 CA GLN A 242 -35.450 1.488 62.968 1.00 74.13 A C ANISOU 1717 CA GLN A 242 7943 8478 11745 -1486 -2636 4133 A C ATOM 1718 C GLN A 242 -36.556 2.291 63.648 1.00 71.31 A C ANISOU 1718 C GLN A 242 7727 8395 10973 -1666 -2531 4136 A C ATOM 1719 O GLN A 242 -36.580 2.414 64.878 1.00 73.47 A O ANISOU 1719 O GLN A 242 8109 8756 11051 -1882 -2679 4213 A O ATOM 1720 CB GLN A 242 -34.409 2.407 62.330 1.00 74.78 A C ANISOU 1720 CB GLN A 242 7852 8516 12045 -1293 -2527 4060 A C ATOM 1721 CG GLN A 242 -33.141 1.678 61.900 1.00 77.67 A C ANISOU 1721 CG GLN A 242 8073 8613 12825 -1152 -2653 4037 A C ATOM 1722 CD GLN A 242 -32.262 2.504 60.979 1.00 79.03 A C ANISOU 1722 CD GLN A 242 8069 8740 13219 -939 -2479 3918 A C ATOM 1723 NE2 GLN A 242 -31.515 1.832 60.110 1.00 79.93 A N ANISOU 1723 NE2 GLN A 242 8048 8640 13680 -774 -2469 3825 A N ATOM 1724 OE1 GLN A 242 -32.250 3.732 61.054 1.00 78.29 A O ANISOU 1724 OE1 GLN A 242 7962 8802 12983 -932 -2352 3899 A O ATOM 1725 N CYS A 243 -37.483 2.848 62.862 1.00 67.12 A N ANISOU 1725 N CYS A 243 7197 8000 10306 -1588 -2270 4038 A N ATOM 1726 CA CYS A 243 -38.583 3.602 63.454 1.00 65.57 A C ANISOU 1726 CA CYS A 243 7121 8062 9730 -1756 -2150 4003 A C ATOM 1727 C CYS A 243 -39.348 2.744 64.457 1.00 67.59 A C ANISOU 1727 C CYS A 243 7549 8365 9767 -2006 -2293 4063 A C ATOM 1728 O CYS A 243 -39.676 3.203 65.558 1.00 67.52 A O ANISOU 1728 O CYS A 243 7646 8519 9490 -2217 -2334 4077 A O ATOM 1729 CB CYS A 243 -39.510 4.131 62.355 1.00 64.36 A C ANISOU 1729 CB CYS A 243 6940 8010 9503 -1630 -1862 3876 A C ATOM 1730 SG CYS A 243 -38.787 5.450 61.347 1.00 63.13 A S ANISOU 1730 SG CYS A 243 6621 7862 9502 -1390 -1665 3793 A S ATOM 1731 N GLU A 244 -39.628 1.486 64.101 1.00 70.62 A N ANISOU 1731 N GLU A 244 7967 8605 10261 -1991 -2368 4092 A N ATOM 1732 CA GLU A 244 -40.280 0.578 65.041 1.00 76.08 A C ANISOU 1732 CA GLU A 244 8827 9317 10762 -2231 -2521 4158 A C ATOM 1733 C GLU A 244 -39.397 0.340 66.259 1.00 80.35 A C ANISOU 1733 C GLU A 244 9421 9790 11318 -2393 -2805 4279 A C ATOM 1734 O GLU A 244 -39.887 0.297 67.397 1.00 81.00 A O ANISOU 1734 O GLU A 244 9657 9992 11126 -2650 -2894 4316 A O ATOM 1735 CB GLU A 244 -40.623 -0.734 64.340 1.00 77.67 A C ANISOU 1735 CB GLU A 244 9042 9355 11116 -2161 -2556 4169 A C ATOM 1736 CG GLU A 244 -41.766 -0.605 63.366 1.00 76.68 A C ANISOU 1736 CG GLU A 244 8914 9322 10898 -2077 -2292 4054 A C ATOM 1737 CD GLU A 244 -41.548 -1.435 62.127 1.00 78.41 A C ANISOU 1737 CD GLU A 244 9039 9337 11417 -1860 -2263 4033 A C ATOM 1738 OE1 GLU A 244 -40.475 -2.066 62.026 1.00 81.17 A O ANISOU 1738 OE1 GLU A 244 9311 9475 12054 -1767 -2439 4091 A O ATOM 1739 OE2 GLU A 244 -42.444 -1.452 61.257 1.00 77.08 A O1- ANISOU 1739 OE2 GLU A 244 8870 9216 11203 -1785 -2064 3945 A O1- ATOM 1740 N GLU A 245 -38.084 0.205 66.030 1.00 87.22 A N ANISOU 1740 N GLU A 245 10163 10465 12512 -2251 -2945 4330 A N ATOM 1741 CA GLU A 245 -37.136 0.003 67.118 1.00 90.27 A C ANISOU 1741 CA GLU A 245 10583 10760 12955 -2389 -3226 4442 A C ATOM 1742 C GLU A 245 -37.149 1.187 68.072 1.00 85.62 A C ANISOU 1742 C GLU A 245 10050 10378 12104 -2546 -3197 4442 A C ATOM 1743 O GLU A 245 -37.118 1.004 69.294 1.00 87.85 A O ANISOU 1743 O GLU A 245 10467 10694 12220 -2789 -3387 4522 A O ATOM 1744 CB GLU A 245 -35.727 -0.204 66.548 1.00 98.77 A C ANISOU 1744 CB GLU A 245 11480 11595 14452 -2179 -3333 4455 A C ATOM 1745 CG GLU A 245 -35.599 -1.384 65.589 1.00106.04 A C ANISOU 1745 CG GLU A 245 12328 12297 15666 -2015 -3363 4433 A C ATOM 1746 CD GLU A 245 -34.210 -1.534 64.969 1.00111.70 A C ANISOU 1746 CD GLU A 245 12850 12783 16809 -1804 -3433 4402 A C ATOM 1747 OE1 GLU A 245 -33.394 -0.591 65.055 1.00112.28 A O ANISOU 1747 OE1 GLU A 245 12825 12877 16958 -1744 -3403 4383 A O ATOM 1748 OE2 GLU A 245 -33.941 -2.610 64.389 1.00115.32 A O1- ANISOU 1748 OE2 GLU A 245 13251 13037 17529 -1702 -3512 4385 A O1- ATOM 1749 N VAL A 246 -37.181 2.412 67.531 1.00 74.33 A N ANISOU 1749 N VAL A 246 8522 9084 10635 -2415 -2963 4349 A N ATOM 1750 CA VAL A 246 -37.198 3.597 68.383 1.00 68.67 A C ANISOU 1750 CA VAL A 246 7847 8569 9675 -2551 -2918 4332 A C ATOM 1751 C VAL A 246 -38.545 3.736 69.096 1.00 68.07 A C ANISOU 1751 C VAL A 246 7943 8721 9200 -2785 -2824 4277 A C ATOM 1752 O VAL A 246 -38.600 4.154 70.257 1.00 74.01 A O ANISOU 1752 O VAL A 246 8799 9597 9723 -3007 -2902 4296 A O ATOM 1753 CB VAL A 246 -36.860 4.871 67.572 1.00 61.03 A C ANISOU 1753 CB VAL A 246 6728 7679 8783 -2342 -2695 4241 A C ATOM 1754 CG1 VAL A 246 -37.031 6.131 68.445 1.00 56.36 A C ANISOU 1754 CG1 VAL A 246 6188 7318 7909 -2489 -2626 4204 A C ATOM 1755 CG2 VAL A 246 -35.455 4.820 66.995 1.00 58.22 A C ANISOU 1755 CG2 VAL A 246 6202 7107 8812 -2137 -2782 4277 A C ATOM 1756 N ALA A 247 -39.653 3.396 68.422 1.00 60.18 A N ANISOU 1756 N ALA A 247 6974 7779 8112 -2746 -2650 4195 A N ATOM 1757 CA ALA A 247 -40.968 3.591 69.039 1.00 58.15 A C ANISOU 1757 CA ALA A 247 6861 7743 7491 -2961 -2528 4107 A C ATOM 1758 C ALA A 247 -41.170 2.699 70.261 1.00 61.01 A C ANISOU 1758 C ALA A 247 7402 8088 7689 -3248 -2753 4195 A C ATOM 1759 O ALA A 247 -41.692 3.156 71.283 1.00 61.82 A O ANISOU 1759 O ALA A 247 7623 8371 7496 -3482 -2736 4150 A O ATOM 1760 CB ALA A 247 -42.078 3.347 68.018 1.00 62.45 A C ANISOU 1760 CB ALA A 247 7390 8330 8007 -2856 -2303 3997 A C ATOM 1761 N ARG A 248 -40.789 1.421 70.176 1.00 65.46 A N ANISOU 1761 N ARG A 248 7994 8438 8440 -3242 -2964 4311 A N ATOM 1762 CA ARG A 248 -40.864 0.561 71.354 1.00 69.75 A C ANISOU 1762 CA ARG A 248 8714 8943 8843 -3522 -3210 4409 A C ATOM 1763 C ARG A 248 -39.947 1.073 72.456 1.00 68.80 A C ANISOU 1763 C ARG A 248 8626 8827 8687 -3667 -3402 4488 A C ATOM 1764 O ARG A 248 -40.333 1.107 73.630 1.00 71.97 A O ANISOU 1764 O ARG A 248 9190 9344 8810 -3954 -3484 4499 A O ATOM 1765 CB ARG A 248 -40.532 -0.886 70.989 1.00 72.96 A C ANISOU 1765 CB ARG A 248 9130 9097 9493 -3466 -3414 4515 A C ATOM 1766 CG ARG A 248 -39.377 -1.060 70.020 1.00 75.33 A C ANISOU 1766 CG ARG A 248 9240 9171 10213 -3173 -3474 4555 A C ATOM 1767 CD ARG A 248 -39.166 -2.534 69.707 1.00 77.64 A C ANISOU 1767 CD ARG A 248 9548 9221 10731 -3134 -3668 4634 A C ATOM 1768 NE ARG A 248 -40.397 -3.182 69.260 1.00 78.19 A N ANISOU 1768 NE ARG A 248 9701 9347 10662 -3163 -3535 4581 A N ATOM 1769 N ALA A 249 -38.723 1.469 72.095 1.00 67.19 A N ANISOU 1769 N ALA A 249 8270 8494 8766 -3480 -3473 4537 A N ATOM 1770 CA ALA A 249 -37.787 1.982 73.088 1.00 73.04 A C ANISOU 1770 CA ALA A 249 9027 9224 9499 -3605 -3655 4612 A C ATOM 1771 C ALA A 249 -38.407 3.119 73.892 1.00 76.49 A C ANISOU 1771 C ALA A 249 9547 9937 9579 -3789 -3507 4521 A C ATOM 1772 O ALA A 249 -38.149 3.253 75.094 1.00 82.90 A O ANISOU 1772 O ALA A 249 10476 10789 10234 -4033 -3672 4577 A O ATOM 1773 CB ALA A 249 -36.498 2.442 72.405 1.00 71.54 A C ANISOU 1773 CB ALA A 249 8635 8887 9661 -3346 -3676 4636 A C ATOM 1774 N LEU A 250 -39.221 3.951 73.246 1.00 59.82 A N ANISOU 1774 N LEU A 250 7212 8932 6585 -1454 -2005 2404 A N ATOM 1775 CA LEU A 250 -39.920 5.032 73.929 1.00 61.31 A C ANISOU 1775 CA LEU A 250 7583 9219 6492 -1375 -1978 2307 A C ATOM 1776 C LEU A 250 -41.303 4.617 74.420 1.00 57.75 A C ANISOU 1776 C LEU A 250 7323 9023 5596 -1384 -1740 2365 A C ATOM 1777 O LEU A 250 -42.029 5.454 74.965 1.00 56.89 A O ANISOU 1777 O LEU A 250 7365 9041 5211 -1295 -1670 2288 A O ATOM 1778 CB LEU A 250 -40.029 6.252 73.007 1.00 63.85 A C ANISOU 1778 CB LEU A 250 7696 9561 7003 -1336 -1843 2215 A C ATOM 1779 CG LEU A 250 -40.131 7.621 73.684 1.00 65.93 A C ANISOU 1779 CG LEU A 250 8124 9795 7133 -1226 -1980 2075 A C ATOM 1780 CD1 LEU A 250 -39.465 8.676 72.818 1.00 63.57 A C ANISOU 1780 CD1 LEU A 250 7590 9362 7202 -1222 -2039 2006 A C ATOM 1781 CD2 LEU A 250 -41.581 7.995 73.950 1.00 66.22 A C ANISOU 1781 CD2 LEU A 250 8308 10091 6761 -1158 -1717 2038 A C ATOM 1782 N GLY A 251 -41.672 3.350 74.260 1.00 58.16 A N ANISOU 1782 N GLY A 251 7374 9153 5573 -1485 -1628 2505 A N ATOM 1783 CA GLY A 251 -42.977 2.873 74.700 1.00 59.06 A C ANISOU 1783 CA GLY A 251 7637 9515 5287 -1523 -1402 2599 A C ATOM 1784 C GLY A 251 -44.164 3.504 74.004 1.00 61.69 A C ANISOU 1784 C GLY A 251 7835 10083 5522 -1505 -1058 2577 A C ATOM 1785 O GLY A 251 -45.196 3.752 74.642 1.00 64.71 A O ANISOU 1785 O GLY A 251 8361 10683 5545 -1464 -904 2588 A O ATOM 1786 N ALA A 252 -44.044 3.771 72.706 1.00 62.59 A N ANISOU 1786 N ALA A 252 7676 10162 5943 -1524 -931 2549 A N ATOM 1787 CA ALA A 252 -45.108 4.370 71.915 1.00 63.93 A C ANISOU 1787 CA ALA A 252 7703 10523 6064 -1507 -625 2522 A C ATOM 1788 C ALA A 252 -45.525 3.417 70.801 1.00 63.80 A C ANISOU 1788 C ALA A 252 7505 10555 6182 -1624 -431 2646 A C ATOM 1789 O ALA A 252 -44.754 2.557 70.367 1.00 66.71 A O ANISOU 1789 O ALA A 252 7805 10766 6775 -1686 -544 2712 A O ATOM 1790 CB ALA A 252 -44.674 5.717 71.321 1.00 62.85 A C ANISOU 1790 CB ALA A 252 7433 10293 6155 -1414 -651 2364 A C ATOM 1791 N ALA A 253 -46.768 3.575 70.341 1.00 62.28 A N ANISOU 1791 N ALA A 253 7237 10537 5890 -1616 -156 2626 A N ATOM 1792 CA ALA A 253 -47.256 2.734 69.252 1.00 61.33 A C ANISOU 1792 CA ALA A 253 6967 10323 6012 -1627 -25 2573 A C ATOM 1793 C ALA A 253 -46.571 3.085 67.938 1.00 59.43 A C ANISOU 1793 C ALA A 253 6525 9970 6084 -1621 -11 2550 A C ATOM 1794 O ALA A 253 -46.271 2.199 67.128 1.00 58.28 A O ANISOU 1794 O ALA A 253 6308 9690 6144 -1634 -31 2560 A O ATOM 1795 CB ALA A 253 -48.772 2.871 69.119 1.00 61.38 A C ANISOU 1795 CB ALA A 253 6965 10405 5949 -1538 185 2435 A C ATOM 1796 N SER A 254 -46.326 4.373 67.706 1.00 56.84 A N ANISOU 1796 N SER A 254 6119 9690 5789 -1587 24 2512 A N ATOM 1797 CA SER A 254 -45.618 4.838 66.524 1.00 52.60 A C ANISOU 1797 CA SER A 254 5382 9028 5575 -1575 43 2477 A C ATOM 1798 C SER A 254 -44.965 6.176 66.846 1.00 49.76 A C ANISOU 1798 C SER A 254 5016 8600 5289 -1504 -84 2364 A C ATOM 1799 O SER A 254 -45.261 6.808 67.863 1.00 49.03 A O ANISOU 1799 O SER A 254 5087 8575 4968 -1442 -158 2293 A O ATOM 1800 CB SER A 254 -46.554 4.954 65.316 1.00 48.96 A C ANISOU 1800 CB SER A 254 4874 8489 5238 -1440 216 2272 A C ATOM 1801 OG SER A 254 -47.516 5.974 65.513 1.00 47.51 A O ANISOU 1801 OG SER A 254 4727 8421 4902 -1371 329 2163 A O ATOM 1802 N LEU A 255 -44.059 6.602 65.964 1.00 48.43 A N ANISOU 1802 N LEU A 255 4671 8276 5455 -1493 -126 2326 A N ATOM 1803 CA LEU A 255 -43.369 7.877 66.137 1.00 50.55 A C ANISOU 1803 CA LEU A 255 4917 8430 5858 -1432 -281 2210 A C ATOM 1804 C LEU A 255 -44.294 9.087 66.122 1.00 52.07 A C ANISOU 1804 C LEU A 255 5159 8737 5886 -1365 -167 2096 A C ATOM 1805 O LEU A 255 -43.845 10.183 66.470 1.00 55.21 A O ANISOU 1805 O LEU A 255 5600 9041 6336 -1307 -334 1993 A O ATOM 1806 CB LEU A 255 -42.303 8.057 65.055 1.00 48.90 A C ANISOU 1806 CB LEU A 255 4472 8059 6047 -1451 -303 2225 A C ATOM 1807 CG LEU A 255 -40.979 7.316 65.245 1.00 54.06 A C ANISOU 1807 CG LEU A 255 5059 8549 6934 -1473 -513 2294 A C ATOM 1808 CD1 LEU A 255 -40.420 7.608 66.632 1.00 55.78 A C ANISOU 1808 CD1 LEU A 255 5448 8676 7069 -1449 -820 2248 A C ATOM 1809 CD2 LEU A 255 -41.144 5.821 65.033 1.00 58.02 A C ANISOU 1809 CD2 LEU A 255 5570 9087 7387 -1509 -436 2405 A C ATOM 1810 N ARG A 256 -45.560 8.936 65.733 1.00 53.39 A N ANISOU 1810 N ARG A 256 5326 9095 5867 -1367 88 2111 A N ATOM 1811 CA ARG A 256 -46.437 10.102 65.707 1.00 55.36 A C ANISOU 1811 CA ARG A 256 5615 9455 5964 -1282 188 1991 A C ATOM 1812 C ARG A 256 -46.752 10.647 67.097 1.00 56.43 A C ANISOU 1812 C ARG A 256 5983 9667 5790 -1180 60 1907 A C ATOM 1813 O ARG A 256 -47.022 11.845 67.238 1.00 57.78 A O ANISOU 1813 O ARG A 256 6217 9848 5888 -1076 24 1773 A O ATOM 1814 CB ARG A 256 -47.741 9.772 64.992 1.00 57.33 A C ANISOU 1814 CB ARG A 256 5829 9832 6123 -1264 449 1977 A C ATOM 1815 CG ARG A 256 -48.753 10.885 65.128 1.00 58.93 A C ANISOU 1815 CG ARG A 256 6083 10180 6129 -1163 551 1859 A C ATOM 1816 CD ARG A 256 -49.483 11.139 63.837 1.00 58.58 A C ANISOU 1816 CD ARG A 256 6013 9963 6283 -1065 655 1688 A C ATOM 1817 NE ARG A 256 -50.262 12.368 63.908 1.00 59.81 A N ANISOU 1817 NE ARG A 256 6185 10250 6288 -980 726 1589 A N ATOM 1818 CZ ARG A 256 -51.329 12.624 63.161 1.00 60.30 A C ANISOU 1818 CZ ARG A 256 6281 10224 6406 -884 822 1448 A C ATOM 1819 NH1 ARG A 256 -51.759 11.736 62.278 1.00 59.70 A N1+ ANISOU 1819 NH1 ARG A 256 6244 9928 6513 -868 856 1397 A N1+ ATOM 1820 NH2 ARG A 256 -51.969 13.775 63.302 1.00 63.44 A N ANISOU 1820 NH2 ARG A 256 6689 10762 6653 -801 873 1365 A N ATOM 1821 N GLU A 257 -46.733 9.807 68.128 1.00 61.11 A N ANISOU 1821 N GLU A 257 6723 10310 6186 -1196 -18 1981 A N ATOM 1822 CA GLU A 257 -47.072 10.243 69.481 1.00 66.54 A C ANISOU 1822 CA GLU A 257 7660 11085 6539 -1082 -122 1911 A C ATOM 1823 C GLU A 257 -45.911 10.891 70.234 1.00 67.26 A C ANISOU 1823 C GLU A 257 7887 10951 6718 -1021 -470 1820 A C ATOM 1824 O GLU A 257 -46.057 11.169 71.431 1.00 68.86 A O ANISOU 1824 O GLU A 257 8335 11191 6636 -915 -600 1763 A O ATOM 1825 CB GLU A 257 -47.626 9.071 70.295 1.00 74.63 A C ANISOU 1825 CB GLU A 257 8805 12271 7280 -1130 -47 2044 A C ATOM 1826 CG GLU A 257 -47.106 7.708 69.880 1.00 80.25 A C ANISOU 1826 CG GLU A 257 9419 12897 8177 -1286 -61 2203 A C ATOM 1827 CD GLU A 257 -48.209 6.808 69.364 1.00 83.31 A C ANISOU 1827 CD GLU A 257 9716 13451 8486 -1366 203 2310 A C ATOM 1828 OE1 GLU A 257 -48.487 5.774 70.007 1.00 86.34 A O ANISOU 1828 OE1 GLU A 257 10205 13823 8776 -1395 185 2354 A O ATOM 1829 OE2 GLU A 257 -48.807 7.142 68.319 1.00 82.89 A O1- ANISOU 1829 OE2 GLU A 257 9516 13353 8625 -1315 357 2190 A O1- ATOM 1830 N VAL A 258 -44.781 11.137 69.574 1.00 64.82 A N ANISOU 1830 N VAL A 258 7427 10414 6789 -1080 -626 1814 A N ATOM 1831 CA VAL A 258 -43.574 11.649 70.213 1.00 67.72 A C ANISOU 1831 CA VAL A 258 7883 10543 7305 -1053 -984 1758 A C ATOM 1832 C VAL A 258 -43.299 13.053 69.693 1.00 66.61 A C ANISOU 1832 C VAL A 258 7680 10283 7348 -1007 -1078 1641 A C ATOM 1833 O VAL A 258 -43.384 13.307 68.486 1.00 67.93 A O ANISOU 1833 O VAL A 258 7628 10452 7731 -1062 -909 1655 A O ATOM 1834 CB VAL A 258 -42.370 10.724 69.952 1.00 66.91 A C ANISOU 1834 CB VAL A 258 7635 10268 7520 -1169 -1120 1872 A C ATOM 1835 CG1 VAL A 258 -41.147 11.187 70.731 1.00 49.38 A C ANISOU 1835 CG1 VAL A 258 5508 7804 5450 -1146 -1515 1827 A C ATOM 1836 CG2 VAL A 258 -42.723 9.277 70.295 1.00 47.35 A C ANISOU 1836 CG2 VAL A 258 5216 7903 4871 -1228 -1016 1997 A C ATOM 1837 N GLN A 259 -42.976 13.960 70.604 1.00 72.30 A N ANISOU 1837 N GLN A 259 8611 10886 7972 -904 -1362 1528 A N ATOM 1838 CA GLN A 259 -42.561 15.307 70.253 1.00 76.21 A C ANISOU 1838 CA GLN A 259 9084 11218 8656 -872 -1538 1425 A C ATOM 1839 C GLN A 259 -41.052 15.442 70.435 1.00 79.18 A C ANISOU 1839 C GLN A 259 9399 11307 9378 -951 -1897 1465 A C ATOM 1840 O GLN A 259 -40.415 14.652 71.135 1.00 77.56 A O ANISOU 1840 O GLN A 259 9255 11029 9187 -980 -2058 1528 A O ATOM 1841 CB GLN A 259 -43.282 16.340 71.124 1.00 80.93 A C ANISOU 1841 CB GLN A 259 9980 11866 8904 -683 -1642 1260 A C ATOM 1842 CG GLN A 259 -44.824 16.363 71.019 1.00 84.06 A C ANISOU 1842 CG GLN A 259 10429 12564 8946 -575 -1297 1208 A C ATOM 1843 CD GLN A 259 -45.531 15.320 71.894 1.00 89.60 A C ANISOU 1843 CD GLN A 259 11269 13489 9286 -534 -1140 1274 A C ATOM 1844 NE2 GLN A 259 -46.641 15.719 72.513 1.00 92.66 A N ANISOU 1844 NE2 GLN A 259 11844 14089 9272 -359 -1017 1183 A N ATOM 1845 OE1 GLN A 259 -45.088 14.179 72.004 1.00 91.31 A O ANISOU 1845 OE1 GLN A 259 11422 13690 9580 -654 -1131 1409 A O ATOM 1846 N LEU A 260 -40.493 16.487 69.818 1.00 84.29 A N ANISOU 1846 N LEU A 260 9930 11788 10308 -989 -2035 1431 A N ATOM 1847 CA LEU A 260 -39.045 16.674 69.799 1.00 87.54 A C ANISOU 1847 CA LEU A 260 10212 11936 11114 -1090 -2355 1496 A C ATOM 1848 C LEU A 260 -38.429 16.589 71.192 1.00 86.66 A C ANISOU 1848 C LEU A 260 10353 11671 10903 -1032 -2737 1463 A C ATOM 1849 O LEU A 260 -37.460 15.855 71.414 1.00 83.06 A O ANISOU 1849 O LEU A 260 9801 11100 10660 -1111 -2893 1561 A O ATOM 1850 CB LEU A 260 -38.716 18.026 69.174 1.00 92.34 A C ANISOU 1850 CB LEU A 260 10736 12391 11957 -1123 -2493 1452 A C ATOM 1851 CG LEU A 260 -37.217 18.286 69.128 1.00 98.63 A C ANISOU 1851 CG LEU A 260 11364 12922 13188 -1246 -2827 1544 A C ATOM 1852 CD1 LEU A 260 -36.501 17.175 68.407 1.00 97.71 A C ANISOU 1852 CD1 LEU A 260 10920 12837 13370 -1369 -2659 1710 A C ATOM 1853 CD2 LEU A 260 -37.035 19.521 68.390 1.00101.26 A C ANISOU 1853 CD2 LEU A 260 11599 13139 13737 -1302 -2905 1528 A C ATOM 1854 N GLU A 261 -38.988 17.328 72.150 1.00 89.56 A N ANISOU 1854 N GLU A 261 11061 12033 10936 -876 -2900 1320 A N ATOM 1855 CA GLU A 261 -38.371 17.405 73.471 1.00 92.58 A C ANISOU 1855 CA GLU A 261 11725 12233 11220 -804 -3308 1274 A C ATOM 1856 C GLU A 261 -38.343 16.044 74.167 1.00 93.64 A C ANISOU 1856 C GLU A 261 11938 12453 11187 -809 -3252 1351 A C ATOM 1857 O GLU A 261 -37.327 15.674 74.770 1.00 95.67 A O ANISOU 1857 O GLU A 261 12233 12514 11604 -852 -3565 1398 A O ATOM 1858 CB GLU A 261 -39.074 18.480 74.301 1.00 94.42 A C ANISOU 1858 CB GLU A 261 12333 12459 11084 -602 -3465 1094 A C ATOM 1859 CG GLU A 261 -40.567 18.285 74.447 1.00 93.99 A C ANISOU 1859 CG GLU A 261 12421 12726 10565 -456 -3094 1024 A C ATOM 1860 CD GLU A 261 -40.957 17.582 75.708 1.00 95.90 A C ANISOU 1860 CD GLU A 261 12965 13076 10395 -333 -3109 1009 A C ATOM 1861 OE1 GLU A 261 -40.090 17.358 76.576 1.00 97.70 A O ANISOU 1861 OE1 GLU A 261 13356 13104 10662 -334 -3453 1023 A O ATOM 1862 OE2 GLU A 261 -42.155 17.278 75.823 1.00 95.68 A O1- ANISOU 1862 OE2 GLU A 261 13011 13338 10003 -236 -2777 989 A O1- ATOM 1863 N GLU A 262 -39.429 15.264 74.051 1.00 93.65 A N ANISOU 1863 N GLU A 262 11953 12739 10892 -780 -2867 1378 A N ATOM 1864 CA GLU A 262 -39.476 13.936 74.659 1.00 89.70 A C ANISOU 1864 CA GLU A 262 11532 12326 10223 -803 -2804 1468 A C ATOM 1865 C GLU A 262 -38.435 13.011 74.038 1.00 78.37 A C ANISOU 1865 C GLU A 262 9804 10779 9195 -968 -2836 1611 A C ATOM 1866 O GLU A 262 -37.863 12.171 74.738 1.00 76.83 A O ANISOU 1866 O GLU A 262 9701 10498 8993 -990 -3013 1668 A O ATOM 1867 CB GLU A 262 -40.870 13.329 74.493 1.00 89.33 A C ANISOU 1867 CB GLU A 262 11507 12608 9825 -770 -2376 1495 A C ATOM 1868 CG GLU A 262 -41.959 14.202 75.077 1.00 93.45 A C ANISOU 1868 CG GLU A 262 12291 13283 9934 -584 -2304 1358 A C ATOM 1869 CD GLU A 262 -43.376 13.762 74.708 1.00 99.15 A C ANISOU 1869 CD GLU A 262 12956 14344 10373 -562 -1857 1393 A C ATOM 1870 OE1 GLU A 262 -43.547 12.854 73.848 1.00100.03 A O ANISOU 1870 OE1 GLU A 262 12816 14556 10636 -705 -1602 1521 A O ATOM 1871 OE2 GLU A 262 -44.321 14.350 75.290 1.00103.44 A O1- ANISOU 1871 OE2 GLU A 262 13712 15051 10540 -389 -1774 1291 A O1- ATOM 1872 N LEU A 263 -38.172 13.151 72.731 1.00 71.14 A N ANISOU 1872 N LEU A 263 8544 9860 8625 -1069 -2669 1667 A N ATOM 1873 CA LEU A 263 -37.153 12.325 72.086 1.00 67.19 A C ANISOU 1873 CA LEU A 263 7752 9264 8514 -1194 -2687 1797 A C ATOM 1874 C LEU A 263 -35.769 12.612 72.649 1.00 72.18 A C ANISOU 1874 C LEU A 263 8375 9611 9437 -1222 -3130 1806 A C ATOM 1875 O LEU A 263 -34.950 11.697 72.765 1.00 77.02 A O ANISOU 1875 O LEU A 263 8887 10140 10236 -1275 -3244 1894 A O ATOM 1876 CB LEU A 263 -37.151 12.543 70.565 1.00 64.26 A C ANISOU 1876 CB LEU A 263 7033 8949 8433 -1274 -2416 1851 A C ATOM 1877 CG LEU A 263 -36.210 11.675 69.721 1.00 51.90 A C ANISOU 1877 CG LEU A 263 5143 7329 7246 -1372 -2359 1985 A C ATOM 1878 CD1 LEU A 263 -36.545 10.201 69.874 1.00 51.18 A C ANISOU 1878 CD1 LEU A 263 5101 7358 6988 -1375 -2208 2057 A C ATOM 1879 CD2 LEU A 263 -36.289 12.059 68.242 1.00 50.05 A C ANISOU 1879 CD2 LEU A 263 4611 7156 7250 -1426 -2084 2027 A C ATOM 1880 N GLU A 264 -35.487 13.870 72.999 1.00 75.56 A N ANISOU 1880 N GLU A 264 8910 9880 9920 -1184 -3406 1717 A N ATOM 1881 CA GLU A 264 -34.177 14.199 73.553 1.00 75.43 A C ANISOU 1881 CA GLU A 264 8886 9575 10200 -1220 -3865 1735 A C ATOM 1882 C GLU A 264 -33.953 13.483 74.877 1.00 74.72 A C ANISOU 1882 C GLU A 264 9095 9405 9892 -1156 -4121 1716 A C ATOM 1883 O GLU A 264 -32.830 13.070 75.185 1.00 76.71 A O ANISOU 1883 O GLU A 264 9262 9465 10419 -1211 -4412 1781 A O ATOM 1884 CB GLU A 264 -34.046 15.710 73.745 1.00 82.04 A C ANISOU 1884 CB GLU A 264 9837 10244 11089 -1187 -4140 1638 A C ATOM 1885 CG GLU A 264 -34.268 16.543 72.485 1.00 84.37 A C ANISOU 1885 CG GLU A 264 9875 10593 11587 -1255 -3925 1653 A C ATOM 1886 CD GLU A 264 -33.054 16.599 71.579 1.00 88.38 A C ANISOU 1886 CD GLU A 264 9969 10968 12644 -1417 -3996 1798 A C ATOM 1887 OE1 GLU A 264 -33.177 17.136 70.456 1.00 87.82 A O ANISOU 1887 OE1 GLU A 264 9661 10953 12752 -1487 -3786 1838 A O ATOM 1888 OE2 GLU A 264 -31.987 16.098 71.986 1.00 90.81 A O1- ANISOU 1888 OE2 GLU A 264 10184 11123 13198 -1468 -4256 1876 A O1- ATOM 1889 N ALA A 265 -35.006 13.361 75.688 1.00 75.63 A N ANISOU 1889 N ALA A 265 9562 9664 9509 -1033 -4025 1632 A N ATOM 1890 CA ALA A 265 -34.893 12.666 76.966 1.00 79.61 A C ANISOU 1890 CA ALA A 265 10387 10110 9752 -967 -4242 1620 A C ATOM 1891 C ALA A 265 -34.450 11.218 76.780 1.00 78.96 A C ANISOU 1891 C ALA A 265 10142 10057 9804 -1062 -4158 1751 A C ATOM 1892 O ALA A 265 -33.678 10.689 77.588 1.00 81.61 A O ANISOU 1892 O ALA A 265 10604 10218 10186 -1063 -4475 1773 A O ATOM 1893 CB ALA A 265 -36.227 12.731 77.708 1.00 79.18 A C ANISOU 1893 CB ALA A 265 10693 10269 9122 -822 -4057 1533 A C ATOM 1894 N ALA A 266 -34.926 10.558 75.723 1.00 77.29 A N ANISOU 1894 N ALA A 266 9666 10048 9651 -1134 -3756 1833 A N ATOM 1895 CA ALA A 266 -34.630 9.152 75.484 1.00 74.70 A C ANISOU 1895 CA ALA A 266 9209 9759 9415 -1206 -3660 1950 A C ATOM 1896 C ALA A 266 -33.375 8.947 74.643 1.00 70.07 A C ANISOU 1896 C ALA A 266 8239 9023 9362 -1293 -3761 2032 A C ATOM 1897 O ALA A 266 -33.199 7.870 74.059 1.00 67.80 A O ANISOU 1897 O ALA A 266 7768 8798 9195 -1339 -3601 2126 A O ATOM 1898 CB ALA A 266 -35.822 8.467 74.812 1.00 74.48 A C ANISOU 1898 CB ALA A 266 9125 10017 9157 -1228 -3197 2002 A C ATOM 1899 N ARG A 267 -32.505 9.957 74.567 1.00 70.62 A N ANISOU 1899 N ARG A 267 8182 8899 9750 -1310 -4027 2006 A N ATOM 1900 CA ARG A 267 -31.311 9.852 73.735 1.00 69.34 A C ANISOU 1900 CA ARG A 267 7617 8620 10108 -1391 -4100 2102 A C ATOM 1901 C ARG A 267 -30.513 8.605 74.087 1.00 70.53 A C ANISOU 1901 C ARG A 267 7727 8685 10387 -1399 -4261 2174 A C ATOM 1902 O ARG A 267 -29.933 7.956 73.208 1.00 72.46 A O ANISOU 1902 O ARG A 267 7642 8956 10933 -1435 -4133 2267 A O ATOM 1903 CB ARG A 267 -30.460 11.110 73.896 1.00 70.62 A C ANISOU 1903 CB ARG A 267 7705 8557 10568 -1421 -4449 2077 A C ATOM 1904 CG ARG A 267 -29.496 11.369 72.754 1.00 68.84 A C ANISOU 1904 CG ARG A 267 7026 8276 10853 -1509 -4370 2176 A C ATOM 1905 CD ARG A 267 -29.386 12.867 72.499 1.00 69.13 A C ANISOU 1905 CD ARG A 267 7041 8204 11021 -1539 -4436 2130 A C ATOM 1906 NE ARG A 267 -28.635 13.179 71.288 1.00 71.63 A N ANISOU 1906 NE ARG A 267 6991 8498 11729 -1601 -4203 2216 A N ATOM 1907 CZ ARG A 267 -28.670 14.360 70.680 1.00 76.69 A C ANISOU 1907 CZ ARG A 267 7550 9103 12485 -1645 -4141 2212 A C ATOM 1908 NH1 ARG A 267 -29.391 15.347 71.196 1.00 76.90 A N1+ ANISOU 1908 NH1 ARG A 267 7827 9097 12294 -1631 -4327 2114 A N1+ ATOM 1909 NH2 ARG A 267 -27.963 14.567 69.578 1.00 78.93 A N ANISOU 1909 NH2 ARG A 267 7538 9378 13075 -1686 -3907 2304 A N ATOM 1910 N ASP A 268 -30.466 8.261 75.373 1.00 70.57 A N ANISOU 1910 N ASP A 268 8079 8580 10153 -1350 -4551 2128 A N ATOM 1911 CA ASP A 268 -29.748 7.091 75.853 1.00 71.35 A C ANISOU 1911 CA ASP A 268 8201 8573 10334 -1349 -4753 2182 A C ATOM 1912 C ASP A 268 -30.560 5.810 75.721 1.00 72.19 A C ANISOU 1912 C ASP A 268 8410 8872 10146 -1344 -4457 2227 A C ATOM 1913 O ASP A 268 -30.038 4.729 76.015 1.00 73.40 A O ANISOU 1913 O ASP A 268 8585 8949 10353 -1344 -4597 2277 A O ATOM 1914 CB ASP A 268 -29.342 7.296 77.316 1.00 68.82 A C ANISOU 1914 CB ASP A 268 8252 8025 9870 -1295 -5175 2100 A C ATOM 1915 CG ASP A 268 -28.276 8.358 77.475 1.00 70.90 A C ANISOU 1915 CG ASP A 268 8427 8024 10487 -1297 -5407 2036 A C ATOM 1916 OD1 ASP A 268 -27.375 8.418 76.613 1.00 70.89 A O ANISOU 1916 OD1 ASP A 268 8044 7962 10927 -1348 -5333 2097 A O ATOM 1917 OD2 ASP A 268 -28.335 9.131 78.455 1.00 74.37 A O1- ANISOU 1917 OD2 ASP A 268 9188 8316 10752 -1241 -5650 1933 A O1- ATOM 1918 N LEU A 269 -31.817 5.908 75.289 1.00 69.27 A N ANISOU 1918 N LEU A 269 8103 8739 9478 -1344 -4073 2215 A N ATOM 1919 CA LEU A 269 -32.657 4.739 75.086 1.00 66.48 A C ANISOU 1919 CA LEU A 269 7829 8570 8861 -1361 -3790 2277 A C ATOM 1920 C LEU A 269 -32.552 4.167 73.681 1.00 66.42 A C ANISOU 1920 C LEU A 269 7462 8660 9116 -1396 -3499 2356 A C ATOM 1921 O LEU A 269 -32.894 2.995 73.477 1.00 65.70 A O ANISOU 1921 O LEU A 269 7404 8649 8909 -1412 -3363 2423 A O ATOM 1922 CB LEU A 269 -34.120 5.097 75.371 1.00 66.09 A C ANISOU 1922 CB LEU A 269 8027 8736 8348 -1341 -3528 2236 A C ATOM 1923 CG LEU A 269 -34.467 5.508 76.802 1.00 69.73 A C ANISOU 1923 CG LEU A 269 8904 9155 8434 -1274 -3748 2161 A C ATOM 1924 CD1 LEU A 269 -35.948 5.816 76.918 1.00 61.14 A C ANISOU 1924 CD1 LEU A 269 7995 8327 6909 -1239 -3425 2135 A C ATOM 1925 CD2 LEU A 269 -34.061 4.424 77.785 1.00 63.82 A C ANISOU 1925 CD2 LEU A 269 8397 8294 7557 -1280 -4002 2209 A C ATOM 1926 N VAL A 270 -32.086 4.959 72.716 1.00 65.47 A N ANISOU 1926 N VAL A 270 7016 8524 9334 -1406 -3414 2355 A N ATOM 1927 CA VAL A 270 -31.989 4.535 71.328 1.00 62.64 A C ANISOU 1927 CA VAL A 270 6326 8262 9211 -1418 -3121 2425 A C ATOM 1928 C VAL A 270 -30.546 4.681 70.851 1.00 62.82 A C ANISOU 1928 C VAL A 270 6006 8133 9730 -1411 -3298 2469 A C ATOM 1929 O VAL A 270 -29.716 5.335 71.484 1.00 59.67 A O ANISOU 1929 O VAL A 270 5595 7560 9516 -1420 -3628 2445 A O ATOM 1930 CB VAL A 270 -32.947 5.318 70.409 1.00 54.30 A C ANISOU 1930 CB VAL A 270 5179 7381 8071 -1434 -2762 2402 A C ATOM 1931 CG1 VAL A 270 -34.363 5.290 70.970 1.00 56.53 A C ANISOU 1931 CG1 VAL A 270 5779 7823 7876 -1433 -2604 2360 A C ATOM 1932 CG2 VAL A 270 -32.464 6.744 70.229 1.00 54.93 A C ANISOU 1932 CG2 VAL A 270 5114 7373 8384 -1449 -2866 2358 A C ATOM 1933 N SER A 271 -30.265 4.047 69.714 1.00 61.11 A N ANISOU 1933 N SER A 271 5508 7986 9724 -1389 -3075 2540 A N ATOM 1934 CA SER A 271 -28.967 4.158 69.065 1.00 57.80 A C ANISOU 1934 CA SER A 271 4725 7472 9765 -1363 -3140 2592 A C ATOM 1935 C SER A 271 -28.827 5.532 68.410 1.00 57.57 A C ANISOU 1935 C SER A 271 4543 7435 9897 -1389 -2978 2561 A C ATOM 1936 O SER A 271 -29.814 6.230 68.165 1.00 56.00 A O ANISOU 1936 O SER A 271 4392 7359 9527 -1441 -2830 2545 A O ATOM 1937 CB SER A 271 -28.789 3.050 68.022 1.00 72.29 A C ANISOU 1937 CB SER A 271 6384 9387 11695 -1286 -2884 2647 A C ATOM 1938 OG SER A 271 -29.683 3.202 66.932 1.00 66.55 A O ANISOU 1938 OG SER A 271 5573 8842 10872 -1295 -2507 2669 A O ATOM 1939 N LYS A 272 -27.578 5.927 68.133 1.00 91.06 A N ANISOU 1939 N LYS A 272 8608 11531 14461 -1355 -3016 2559 A N ATOM 1940 CA LYS A 272 -27.335 7.228 67.506 1.00 97.64 A C ANISOU 1940 CA LYS A 272 9317 12336 15445 -1384 -2888 2548 A C ATOM 1941 C LYS A 272 -28.072 7.352 66.180 1.00 89.89 A C ANISOU 1941 C LYS A 272 8239 11535 14380 -1363 -2458 2558 A C ATOM 1942 O LYS A 272 -28.732 8.362 65.912 1.00 90.44 A O ANISOU 1942 O LYS A 272 8352 11651 14361 -1412 -2357 2527 A O ATOM 1943 CB LYS A 272 -25.839 7.458 67.290 1.00 62.01 A C ANISOU 1943 CB LYS A 272 4608 7672 11281 -1354 -2964 2580 A C ATOM 1944 CG LYS A 272 -25.045 7.698 68.563 1.00 66.45 A C ANISOU 1944 CG LYS A 272 5276 8013 11957 -1386 -3398 2560 A C ATOM 1945 CD LYS A 272 -23.592 8.069 68.284 1.00 71.85 A C ANISOU 1945 CD LYS A 272 5738 8559 13002 -1376 -3456 2613 A C ATOM 1946 CE LYS A 272 -22.823 8.231 69.589 1.00 76.73 A C ANISOU 1946 CE LYS A 272 6486 8936 13733 -1406 -3901 2591 A C ATOM 1947 NZ LYS A 272 -21.405 8.614 69.362 1.00 80.50 A N1+ ANISOU 1947 NZ LYS A 272 6733 9279 14574 -1413 -3977 2662 A N1+ ATOM 1948 N GLU A 273 -27.955 6.342 65.322 1.00 96.23 A N ANISOU 1948 N GLU A 273 8933 12426 15205 -1277 -2215 2591 A N ATOM 1949 CA GLU A 273 -28.700 6.370 64.067 1.00 89.14 A C ANISOU 1949 CA GLU A 273 8005 11678 14188 -1237 -1819 2583 A C ATOM 1950 C GLU A 273 -30.205 6.406 64.303 1.00 80.28 A C ANISOU 1950 C GLU A 273 7059 10688 12755 -1300 -1742 2562 A C ATOM 1951 O GLU A 273 -30.924 7.184 63.668 1.00 72.71 A O ANISOU 1951 O GLU A 273 6135 9802 11691 -1313 -1525 2521 A O ATOM 1952 CB GLU A 273 -28.347 5.161 63.205 1.00 88.91 A C ANISOU 1952 CB GLU A 273 7872 11703 14205 -1118 -1624 2616 A C ATOM 1953 CG GLU A 273 -29.185 5.088 61.927 1.00 90.90 A C ANISOU 1953 CG GLU A 273 8156 12087 14296 -1060 -1243 2591 A C ATOM 1954 CD GLU A 273 -28.664 4.060 60.934 1.00 94.59 A C ANISOU 1954 CD GLU A 273 8516 12587 14838 -922 -1063 2617 A C ATOM 1955 OE1 GLU A 273 -27.625 3.438 61.243 1.00 91.48 A O ANISOU 1955 OE1 GLU A 273 7996 12127 14636 -871 -1223 2656 A O ATOM 1956 OE2 GLU A 273 -29.256 3.906 59.837 1.00102.44 A O1- ANISOU 1956 OE2 GLU A 273 9558 13663 15702 -855 -779 2589 A O1- ATOM 1957 N GLY A 274 -30.698 5.563 65.210 1.00 77.53 A N ANISOU 1957 N GLY A 274 6833 10381 12244 -1340 -1926 2593 A N ATOM 1958 CA GLY A 274 -32.122 5.549 65.520 1.00 73.95 A C ANISOU 1958 CA GLY A 274 6543 10085 11469 -1415 -1861 2593 A C ATOM 1959 C GLY A 274 -32.649 6.884 66.008 1.00 68.59 A C ANISOU 1959 C GLY A 274 5997 9399 10663 -1468 -1924 2515 A C ATOM 1960 O GLY A 274 -33.793 7.254 65.724 1.00 48.39 A O ANISOU 1960 O GLY A 274 3560 6967 7858 -1478 -1699 2468 A O ATOM 1961 N PHE A 275 -31.833 7.618 66.764 1.00 68.84 A N ANISOU 1961 N PHE A 275 6020 9274 10862 -1496 -2252 2496 A N ATOM 1962 CA PHE A 275 -32.273 8.920 67.247 1.00 52.36 A C ANISOU 1962 CA PHE A 275 4084 7153 8656 -1527 -2356 2412 A C ATOM 1963 C PHE A 275 -32.449 9.894 66.092 1.00 51.25 A C ANISOU 1963 C PHE A 275 3746 7064 8662 -1559 -2121 2420 A C ATOM 1964 O PHE A 275 -33.431 10.644 66.047 1.00 61.24 A O ANISOU 1964 O PHE A 275 5153 8409 9708 -1565 -2011 2348 A O ATOM 1965 CB PHE A 275 -31.282 9.468 68.272 1.00 60.08 A C ANISOU 1965 CB PHE A 275 5106 7917 9805 -1548 -2800 2396 A C ATOM 1966 CG PHE A 275 -31.598 10.859 68.730 1.00 60.72 A C ANISOU 1966 CG PHE A 275 5346 7927 9799 -1567 -2957 2309 A C ATOM 1967 CD1 PHE A 275 -31.110 11.964 68.048 1.00 62.04 A C ANISOU 1967 CD1 PHE A 275 5311 8015 10247 -1620 -2958 2330 A C ATOM 1968 CD2 PHE A 275 -32.389 11.062 69.845 1.00 60.74 A C ANISOU 1968 CD2 PHE A 275 5737 7934 9407 -1510 -3080 2197 A C ATOM 1969 CE1 PHE A 275 -31.413 13.243 68.474 1.00 63.44 A C ANISOU 1969 CE1 PHE A 275 5636 8115 10355 -1643 -3162 2257 A C ATOM 1970 CE2 PHE A 275 -32.691 12.331 70.276 1.00 63.22 A C ANISOU 1970 CE2 PHE A 275 6224 8177 9619 -1496 -3239 2103 A C ATOM 1971 CZ PHE A 275 -32.201 13.425 69.593 1.00 63.62 A C ANISOU 1971 CZ PHE A 275 6061 8136 9976 -1562 -3295 2127 A C ATOM 1972 N ARG A 276 -31.511 9.897 65.145 1.00 51.63 A N ANISOU 1972 N ARG A 276 3634 7026 8959 -1500 -1952 2436 A N ATOM 1973 CA ARG A 276 -31.634 10.796 64.004 1.00 52.51 A C ANISOU 1973 CA ARG A 276 3684 7151 9116 -1478 -1687 2402 A C ATOM 1974 C ARG A 276 -32.858 10.447 63.171 1.00 53.11 A C ANISOU 1974 C ARG A 276 3828 7404 8949 -1439 -1333 2368 A C ATOM 1975 O ARG A 276 -33.561 11.336 62.674 1.00 52.98 A O ANISOU 1975 O ARG A 276 3862 7431 8837 -1449 -1193 2311 A O ATOM 1976 CB ARG A 276 -30.387 10.721 63.129 1.00 53.61 A C ANISOU 1976 CB ARG A 276 3655 7202 9513 -1411 -1577 2437 A C ATOM 1977 CG ARG A 276 -29.100 11.222 63.752 1.00 54.75 A C ANISOU 1977 CG ARG A 276 3711 7163 9929 -1450 -1884 2479 A C ATOM 1978 CD ARG A 276 -28.041 11.236 62.674 1.00 55.79 A C ANISOU 1978 CD ARG A 276 3656 7269 10273 -1390 -1702 2527 A C ATOM 1979 NE ARG A 276 -27.478 9.903 62.499 1.00 69.21 A N ANISOU 1979 NE ARG A 276 5262 9003 12032 -1304 -1635 2563 A N ATOM 1980 CZ ARG A 276 -26.916 9.469 61.375 1.00 66.04 A C ANISOU 1980 CZ ARG A 276 4727 8656 11708 -1213 -1388 2589 A C ATOM 1981 NH1 ARG A 276 -26.844 10.260 60.310 1.00 62.08 A N1+ ANISOU 1981 NH1 ARG A 276 4180 8184 11222 -1201 -1179 2584 A N1+ ATOM 1982 NH2 ARG A 276 -26.439 8.234 61.313 1.00 64.56 A N ANISOU 1982 NH2 ARG A 276 4462 8494 11573 -1129 -1366 2617 A N ATOM 1983 N ARG A 277 -33.115 9.151 62.998 1.00 53.16 A N ANISOU 1983 N ARG A 277 3850 7495 8854 -1390 -1202 2399 A N ATOM 1984 CA ARG A 277 -34.296 8.713 62.266 1.00 50.65 A C ANISOU 1984 CA ARG A 277 3632 7320 8291 -1347 -895 2364 A C ATOM 1985 C ARG A 277 -35.560 9.295 62.882 1.00 50.64 A C ANISOU 1985 C ARG A 277 3751 7443 8047 -1433 -914 2341 A C ATOM 1986 O ARG A 277 -36.397 9.875 62.181 1.00 53.77 A O ANISOU 1986 O ARG A 277 4219 7898 8314 -1402 -694 2265 A O ATOM 1987 CB ARG A 277 -34.345 7.185 62.245 1.00 50.94 A C ANISOU 1987 CB ARG A 277 3681 7409 8264 -1307 -845 2424 A C ATOM 1988 CG ARG A 277 -33.144 6.558 61.550 1.00 45.45 A C ANISOU 1988 CG ARG A 277 2853 6620 7795 -1205 -810 2447 A C ATOM 1989 CD ARG A 277 -32.907 7.164 60.173 1.00 55.40 A C ANISOU 1989 CD ARG A 277 4083 7852 9114 -1113 -563 2372 A C ATOM 1990 NE ARG A 277 -31.483 7.318 59.878 1.00 57.40 A N ANISOU 1990 NE ARG A 277 4163 8007 9639 -1072 -626 2407 A N ATOM 1991 CZ ARG A 277 -30.713 6.367 59.355 1.00 58.52 A C ANISOU 1991 CZ ARG A 277 4201 8139 9895 -978 -570 2449 A C ATOM 1992 NH1 ARG A 277 -31.221 5.176 59.072 1.00 58.00 A N1+ ANISOU 1992 NH1 ARG A 277 4195 8136 9705 -916 -472 2466 A N1+ ATOM 1993 NH2 ARG A 277 -29.428 6.605 59.124 1.00 60.07 A N ANISOU 1993 NH2 ARG A 277 4226 8264 10334 -948 -621 2485 A N ATOM 1994 N ALA A 278 -35.716 9.146 64.199 1.00 52.86 A N ANISOU 1994 N ALA A 278 4114 7753 8217 -1508 -1181 2372 A N ATOM 1995 CA ALA A 278 -36.904 9.656 64.873 1.00 52.22 A C ANISOU 1995 CA ALA A 278 4307 7760 7776 -1493 -1159 2271 A C ATOM 1996 C ALA A 278 -36.982 11.176 64.815 1.00 53.79 A C ANISOU 1996 C ALA A 278 4509 7908 8023 -1503 -1229 2193 A C ATOM 1997 O ALA A 278 -38.082 11.735 64.731 1.00 54.63 A O ANISOU 1997 O ALA A 278 4745 8122 7888 -1475 -1082 2113 A O ATOM 1998 CB ALA A 278 -36.923 9.185 66.327 1.00 51.73 A C ANISOU 1998 CB ALA A 278 4503 7665 7485 -1470 -1404 2241 A C ATOM 1999 N ARG A 279 -35.838 11.862 64.859 1.00 54.29 A N ANISOU 1999 N ARG A 279 4427 7802 8398 -1543 -1467 2219 A N ATOM 2000 CA ARG A 279 -35.856 13.320 64.807 1.00 55.39 A C ANISOU 2000 CA ARG A 279 4583 7862 8600 -1566 -1578 2155 A C ATOM 2001 C ARG A 279 -36.434 13.813 63.488 1.00 54.52 A C ANISOU 2001 C ARG A 279 4336 7845 8533 -1586 -1267 2162 A C ATOM 2002 O ARG A 279 -37.157 14.816 63.452 1.00 53.62 A O ANISOU 2002 O ARG A 279 4347 7748 8278 -1569 -1250 2068 A O ATOM 2003 CB ARG A 279 -34.449 13.877 65.016 1.00 53.43 A C ANISOU 2003 CB ARG A 279 4171 7405 8725 -1632 -1903 2216 A C ATOM 2004 CG ARG A 279 -34.389 15.396 64.998 1.00 52.16 A C ANISOU 2004 CG ARG A 279 4042 7128 8649 -1672 -2076 2164 A C ATOM 2005 CD ARG A 279 -33.076 15.909 65.561 1.00 57.01 A C ANISOU 2005 CD ARG A 279 4614 7499 9549 -1714 -2450 2198 A C ATOM 2006 NE ARG A 279 -31.934 15.440 64.783 1.00 59.58 A N ANISOU 2006 NE ARG A 279 4756 7747 10132 -1685 -2271 2275 A N ATOM 2007 CZ ARG A 279 -30.668 15.591 65.154 1.00 60.65 A C ANISOU 2007 CZ ARG A 279 4833 7694 10518 -1700 -2505 2324 A C ATOM 2008 NH1 ARG A 279 -30.379 16.199 66.296 1.00 64.01 A N1+ ANISOU 2008 NH1 ARG A 279 5399 7951 10971 -1739 -2929 2291 A N1+ ATOM 2009 NH2 ARG A 279 -29.690 15.130 64.385 1.00 61.98 A N ANISOU 2009 NH2 ARG A 279 4821 7841 10889 -1662 -2325 2398 A N ATOM 2010 N HIS A 280 -36.119 13.125 62.390 1.00 53.15 A N ANISOU 2010 N HIS A 280 4089 7663 8444 -1514 -983 2177 A N ATOM 2011 CA HIS A 280 -36.698 13.479 61.099 1.00 52.69 A C ANISOU 2011 CA HIS A 280 4080 7630 8310 -1436 -667 2093 A C ATOM 2012 C HIS A 280 -38.213 13.310 61.112 1.00 53.22 A C ANISOU 2012 C HIS A 280 4273 7875 8075 -1424 -489 2044 A C ATOM 2013 O HIS A 280 -38.955 14.233 60.754 1.00 52.80 A O ANISOU 2013 O HIS A 280 4270 7856 7936 -1425 -411 1975 A O ATOM 2014 CB HIS A 280 -36.066 12.630 59.996 1.00 54.87 A C ANISOU 2014 CB HIS A 280 4327 7856 8664 -1325 -456 2077 A C ATOM 2015 CG HIS A 280 -36.861 12.597 58.730 1.00 55.56 A C ANISOU 2015 CG HIS A 280 4529 7981 8601 -1230 -164 1964 A C ATOM 2016 CD2 HIS A 280 -37.670 11.644 58.209 1.00 53.67 A C ANISOU 2016 CD2 HIS A 280 4409 7808 8176 -1150 27 1902 A C ATOM 2017 ND1 HIS A 280 -36.873 13.643 57.832 1.00 56.03 A N ANISOU 2017 ND1 HIS A 280 4602 7986 8702 -1218 -80 1893 A N ATOM 2018 CE1 HIS A 280 -37.657 13.336 56.814 1.00 54.09 A C ANISOU 2018 CE1 HIS A 280 4483 7769 8301 -1133 143 1782 A C ATOM 2019 NE2 HIS A 280 -38.150 12.128 57.017 1.00 52.81 A N ANISOU 2019 NE2 HIS A 280 4390 7669 8006 -1088 204 1780 A N ATOM 2020 N VAL A 281 -38.692 12.133 61.522 1.00 52.07 A N ANISOU 2020 N VAL A 281 4180 7844 7761 -1415 -426 2084 A N ATOM 2021 CA VAL A 281 -40.127 11.846 61.482 1.00 46.26 A C ANISOU 2021 CA VAL A 281 3578 7276 6721 -1390 -229 2040 A C ATOM 2022 C VAL A 281 -40.906 12.893 62.269 1.00 45.82 A C ANISOU 2022 C VAL A 281 3585 7337 6489 -1441 -324 2006 A C ATOM 2023 O VAL A 281 -41.824 13.534 61.746 1.00 50.49 A O ANISOU 2023 O VAL A 281 4210 8007 6966 -1416 -163 1939 A O ATOM 2024 CB VAL A 281 -40.411 10.428 62.004 1.00 44.68 A C ANISOU 2024 CB VAL A 281 3433 7174 6369 -1400 -203 2117 A C ATOM 2025 CG1 VAL A 281 -41.909 10.196 62.093 1.00 37.41 A C ANISOU 2025 CG1 VAL A 281 2667 6424 5123 -1376 -21 2073 A C ATOM 2026 CG2 VAL A 281 -39.764 9.399 61.097 1.00 37.99 A C ANISOU 2026 CG2 VAL A 281 2586 6197 5651 -1298 -110 2098 A C ATOM 2027 N VAL A 282 -40.552 13.075 63.543 1.00 51.41 A N ANISOU 2027 N VAL A 282 4449 7980 7106 -1417 -599 1962 A N ATOM 2028 CA VAL A 282 -41.270 14.028 64.385 1.00 52.80 A C ANISOU 2028 CA VAL A 282 4856 8188 7015 -1341 -708 1828 A C ATOM 2029 C VAL A 282 -41.246 15.412 63.750 1.00 59.60 A C ANISOU 2029 C VAL A 282 5667 8968 8012 -1343 -740 1758 A C ATOM 2030 O VAL A 282 -42.233 16.156 63.807 1.00 63.26 A O ANISOU 2030 O VAL A 282 6267 9515 8254 -1269 -674 1646 A O ATOM 2031 CB VAL A 282 -40.676 14.042 65.807 1.00 49.91 A C ANISOU 2031 CB VAL A 282 4675 7721 6567 -1307 -1042 1796 A C ATOM 2032 CG1 VAL A 282 -41.287 15.167 66.635 1.00 49.45 A C ANISOU 2032 CG1 VAL A 282 4870 7669 6249 -1200 -1186 1646 A C ATOM 2033 CG2 VAL A 282 -40.888 12.699 66.492 1.00 48.73 A C ANISOU 2033 CG2 VAL A 282 4623 7669 6224 -1302 -1002 1859 A C ATOM 2034 N GLY A 283 -40.114 15.786 63.147 1.00 59.12 A N ANISOU 2034 N GLY A 283 5405 8743 8316 -1428 -849 1831 A N ATOM 2035 CA GLY A 283 -40.025 17.078 62.491 1.00 58.84 A C ANISOU 2035 CA GLY A 283 5314 8613 8429 -1457 -891 1791 A C ATOM 2036 C GLY A 283 -40.710 17.133 61.142 1.00 56.26 A C ANISOU 2036 C GLY A 283 4869 8386 8123 -1472 -561 1807 A C ATOM 2037 O GLY A 283 -41.254 18.177 60.768 1.00 55.70 A O ANISOU 2037 O GLY A 283 4861 8301 8002 -1453 -546 1722 A O ATOM 2038 N GLU A 284 -40.699 16.025 60.396 1.00 55.03 A N ANISOU 2038 N GLU A 284 4645 8272 7994 -1445 -307 1856 A N ATOM 2039 CA GLU A 284 -41.397 15.991 59.114 1.00 51.65 A C ANISOU 2039 CA GLU A 284 4330 7818 7477 -1328 -18 1733 A C ATOM 2040 C GLU A 284 -42.907 16.041 59.307 1.00 50.88 A C ANISOU 2040 C GLU A 284 4335 7906 7092 -1296 117 1674 A C ATOM 2041 O GLU A 284 -43.611 16.745 58.572 1.00 51.57 A O ANISOU 2041 O GLU A 284 4485 7980 7129 -1250 228 1576 A O ATOM 2042 CB GLU A 284 -40.992 14.742 58.329 1.00 49.00 A C ANISOU 2042 CB GLU A 284 4048 7401 7170 -1227 139 1695 A C ATOM 2043 CG GLU A 284 -41.574 14.670 56.928 1.00 49.23 A C ANISOU 2043 CG GLU A 284 4205 7362 7137 -1122 357 1544 A C ATOM 2044 CD GLU A 284 -40.880 15.600 55.958 1.00 49.14 A C ANISOU 2044 CD GLU A 284 4152 7230 7288 -1128 366 1510 A C ATOM 2045 OE1 GLU A 284 -40.073 16.436 56.414 1.00 52.31 A O ANISOU 2045 OE1 GLU A 284 4430 7591 7854 -1212 198 1600 A O ATOM 2046 OE2 GLU A 284 -41.141 15.497 54.741 1.00 47.35 A O1- ANISOU 2046 OE2 GLU A 284 4020 6946 7023 -1060 516 1399 A O1- ATOM 2047 N ILE A 285 -43.425 15.305 60.293 1.00 51.63 A N ANISOU 2047 N ILE A 285 4448 8185 6983 -1320 111 1736 A N ATOM 2048 CA ILE A 285 -44.857 15.356 60.574 1.00 46.67 A C ANISOU 2048 CA ILE A 285 3918 7769 6044 -1277 255 1682 A C ATOM 2049 C ILE A 285 -45.273 16.785 60.882 1.00 48.58 A C ANISOU 2049 C ILE A 285 4271 8003 6185 -1216 137 1549 A C ATOM 2050 O ILE A 285 -46.314 17.264 60.415 1.00 51.98 A O ANISOU 2050 O ILE A 285 4740 8528 6480 -1160 288 1469 A O ATOM 2051 CB ILE A 285 -45.214 14.405 61.733 1.00 42.97 A C ANISOU 2051 CB ILE A 285 3559 7440 5327 -1260 231 1719 A C ATOM 2052 CG1 ILE A 285 -44.942 12.950 61.346 1.00 41.58 A C ANISOU 2052 CG1 ILE A 285 3384 7190 5225 -1252 313 1775 A C ATOM 2053 CG2 ILE A 285 -46.671 14.584 62.138 1.00 39.58 A C ANISOU 2053 CG2 ILE A 285 3271 7214 4554 -1171 367 1634 A C ATOM 2054 CD1 ILE A 285 -45.248 11.951 62.450 1.00 43.89 A C ANISOU 2054 CD1 ILE A 285 3727 7658 5293 -1302 298 1883 A C ATOM 2055 N ARG A 286 -44.454 17.491 61.662 1.00 51.73 A N ANISOU 2055 N ARG A 286 4749 8257 6650 -1207 -162 1506 A N ATOM 2056 CA ARG A 286 -44.770 18.864 62.034 1.00 53.25 A C ANISOU 2056 CA ARG A 286 5104 8391 6736 -1121 -336 1358 A C ATOM 2057 C ARG A 286 -44.627 19.802 60.842 1.00 52.79 A C ANISOU 2057 C ARG A 286 4937 8221 6899 -1178 -303 1349 A C ATOM 2058 O ARG A 286 -45.391 20.764 60.708 1.00 52.68 A O ANISOU 2058 O ARG A 286 5040 8224 6753 -1096 -310 1221 A O ATOM 2059 CB ARG A 286 -43.874 19.286 63.199 1.00 56.49 A C ANISOU 2059 CB ARG A 286 5648 8647 7169 -1101 -703 1326 A C ATOM 2060 CG ARG A 286 -43.842 20.762 63.521 1.00 61.29 A C ANISOU 2060 CG ARG A 286 6421 9115 7749 -1031 -971 1191 A C ATOM 2061 CD ARG A 286 -42.545 21.393 63.013 1.00 67.26 A C ANISOU 2061 CD ARG A 286 7032 9620 8903 -1173 -1196 1274 A C ATOM 2062 NE ARG A 286 -42.140 22.537 63.819 1.00 73.17 A N ANISOU 2062 NE ARG A 286 7983 10179 9641 -1122 -1593 1175 A N ATOM 2063 CZ ARG A 286 -41.109 23.328 63.549 1.00 78.76 A C ANISOU 2063 CZ ARG A 286 8610 10649 10665 -1239 -1860 1234 A C ATOM 2064 NH1 ARG A 286 -40.821 24.345 64.355 1.00 82.41 A N1+ ANISOU 2064 NH1 ARG A 286 9295 10927 11091 -1184 -2254 1137 A N1+ ATOM 2065 NH2 ARG A 286 -40.378 23.108 62.472 1.00 79.41 A N ANISOU 2065 NH2 ARG A 286 8396 10681 11097 -1408 -1736 1396 A N ATOM 2066 N ARG A 287 -43.670 19.527 59.954 1.00 48.76 A N ANISOU 2066 N ARG A 287 4207 7603 6718 -1309 -261 1487 A N ATOM 2067 CA ARG A 287 -43.526 20.343 58.753 1.00 47.77 A C ANISOU 2067 CA ARG A 287 3973 7380 6796 -1375 -200 1505 A C ATOM 2068 C ARG A 287 -44.699 20.146 57.800 1.00 48.84 A C ANISOU 2068 C ARG A 287 4100 7656 6800 -1334 114 1470 A C ATOM 2069 O ARG A 287 -45.196 21.113 57.210 1.00 46.87 A O ANISOU 2069 O ARG A 287 3904 7369 6537 -1314 128 1390 A O ATOM 2070 CB ARG A 287 -42.215 20.008 58.047 1.00 45.43 A C ANISOU 2070 CB ARG A 287 3512 6925 6825 -1456 -193 1625 A C ATOM 2071 CG ARG A 287 -40.995 20.691 58.627 1.00 48.98 A C ANISOU 2071 CG ARG A 287 3863 7214 7532 -1573 -538 1711 A C ATOM 2072 CD ARG A 287 -39.795 20.452 57.732 1.00 47.33 A C ANISOU 2072 CD ARG A 287 3625 6829 7528 -1533 -444 1732 A C ATOM 2073 NE ARG A 287 -39.456 19.034 57.672 1.00 47.86 A N ANISOU 2073 NE ARG A 287 3693 6938 7553 -1447 -285 1739 A N ATOM 2074 CZ ARG A 287 -38.653 18.423 58.536 1.00 52.46 A C ANISOU 2074 CZ ARG A 287 4200 7501 8233 -1481 -449 1824 A C ATOM 2075 NH1 ARG A 287 -38.107 19.108 59.533 1.00 53.75 A N1+ ANISOU 2075 NH1 ARG A 287 4302 7586 8536 -1591 -796 1890 A N1+ ATOM 2076 NH2 ARG A 287 -38.402 17.126 58.408 1.00 51.48 A N ANISOU 2076 NH2 ARG A 287 4081 7413 8068 -1405 -309 1830 A N ATOM 2077 N THR A 288 -45.157 18.902 57.638 1.00 48.39 A N ANISOU 2077 N THR A 288 4136 7639 6611 -1231 318 1430 A N ATOM 2078 CA THR A 288 -46.263 18.635 56.724 1.00 46.47 A C ANISOU 2078 CA THR A 288 4048 7366 6242 -1105 534 1287 A C ATOM 2079 C THR A 288 -47.516 19.382 57.162 1.00 48.74 A C ANISOU 2079 C THR A 288 4343 7879 6296 -1087 566 1248 A C ATOM 2080 O THR A 288 -48.179 20.038 56.351 1.00 48.85 A O ANISOU 2080 O THR A 288 4413 7846 6300 -1039 641 1154 A O ATOM 2081 CB THR A 288 -46.525 17.129 56.634 1.00 44.67 A C ANISOU 2081 CB THR A 288 3933 7097 5942 -1021 645 1243 A C ATOM 2082 CG2 THR A 288 -47.641 16.838 55.637 1.00 39.88 A C ANISOU 2082 CG2 THR A 288 3485 6396 5271 -919 795 1090 A C ATOM 2083 OG1 THR A 288 -45.332 16.458 56.207 1.00 43.83 A O ANISOU 2083 OG1 THR A 288 3799 6839 6015 -1031 620 1269 A O ATOM 2084 N ALA A 289 -47.854 19.293 58.450 1.00 48.72 A N ANISOU 2084 N ALA A 289 4331 8110 6069 -1088 503 1278 A N ATOM 2085 CA ALA A 289 -48.990 20.050 58.965 1.00 48.12 A C ANISOU 2085 CA ALA A 289 4421 8149 5714 -942 489 1115 A C ATOM 2086 C ALA A 289 -48.788 21.547 58.755 1.00 50.37 A C ANISOU 2086 C ALA A 289 4796 8272 6070 -905 290 995 A C ATOM 2087 O ALA A 289 -49.744 22.276 58.463 1.00 54.86 A O ANISOU 2087 O ALA A 289 5444 8895 6503 -805 341 870 A O ATOM 2088 CB ALA A 289 -49.205 19.732 60.444 1.00 50.34 A C ANISOU 2088 CB ALA A 289 4846 8552 5728 -845 390 1075 A C ATOM 2089 N GLN A 290 -47.548 22.026 58.902 1.00 49.95 A N ANISOU 2089 N GLN A 290 4731 8011 6237 -986 45 1038 A N ATOM 2090 CA GLN A 290 -47.276 23.442 58.672 1.00 48.58 A C ANISOU 2090 CA GLN A 290 4646 7654 6159 -980 -178 948 A C ATOM 2091 C GLN A 290 -47.404 23.798 57.196 1.00 46.91 A C ANISOU 2091 C GLN A 290 4318 7378 6128 -1064 -20 987 A C ATOM 2092 O GLN A 290 -47.917 24.870 56.852 1.00 48.72 A O ANISOU 2092 O GLN A 290 4658 7547 6308 -1007 -92 869 A O ATOM 2093 CB GLN A 290 -45.878 23.811 59.167 1.00 47.35 A C ANISOU 2093 CB GLN A 290 4480 7283 6226 -1075 -494 1016 A C ATOM 2094 CG GLN A 290 -45.757 24.145 60.642 1.00 51.53 A C ANISOU 2094 CG GLN A 290 5229 7784 6566 -959 -788 913 A C ATOM 2095 CD GLN A 290 -44.300 24.215 61.083 1.00 55.23 A C ANISOU 2095 CD GLN A 290 5645 8042 7299 -1080 -1086 1018 A C ATOM 2096 NE2 GLN A 290 -44.071 24.602 62.330 1.00 57.78 A N ANISOU 2096 NE2 GLN A 290 6181 8287 7484 -986 -1396 929 A N ATOM 2097 OE1 GLN A 290 -43.391 23.949 60.296 1.00 54.39 A O ANISOU 2097 OE1 GLN A 290 5308 7840 7516 -1248 -1041 1178 A O ATOM 2098 N ALA A 291 -46.957 22.908 56.308 1.00 41.51 A N ANISOU 2098 N ALA A 291 3431 6702 5640 -1186 191 1148 A N ATOM 2099 CA ALA A 291 -46.997 23.208 54.881 1.00 40.63 A C ANISOU 2099 CA ALA A 291 3224 6520 5695 -1261 346 1198 A C ATOM 2100 C ALA A 291 -48.428 23.253 54.362 1.00 43.84 A C ANISOU 2100 C ALA A 291 3713 7050 5894 -1154 543 1083 A C ATOM 2101 O ALA A 291 -48.753 24.072 53.494 1.00 48.14 A O ANISOU 2101 O ALA A 291 4288 7517 6485 -1164 560 1037 A O ATOM 2102 CB ALA A 291 -46.176 22.179 54.106 1.00 32.45 A C ANISOU 2102 CB ALA A 291 2248 5284 4798 -1206 475 1187 A C ATOM 2103 N ALA A 292 -49.294 22.371 54.863 1.00 41.65 A N ANISOU 2103 N ALA A 292 3509 6919 5398 -1038 672 1022 A N ATOM 2104 CA ALA A 292 -50.700 22.435 54.483 1.00 39.10 A C ANISOU 2104 CA ALA A 292 3294 6668 4896 -911 811 893 A C ATOM 2105 C ALA A 292 -51.315 23.766 54.896 1.00 42.29 A C ANISOU 2105 C ALA A 292 3758 7178 5132 -840 686 766 A C ATOM 2106 O ALA A 292 -52.043 24.391 54.118 1.00 42.47 A O ANISOU 2106 O ALA A 292 3823 7181 5135 -796 741 680 A O ATOM 2107 CB ALA A 292 -51.469 21.266 55.097 1.00 37.24 A C ANISOU 2107 CB ALA A 292 3153 6503 4493 -802 900 853 A C ATOM 2108 N ALA A 293 -51.021 24.221 56.116 1.00 44.10 A N ANISOU 2108 N ALA A 293 4112 7399 5246 -763 456 688 A N ATOM 2109 CA ALA A 293 -51.533 25.512 56.563 1.00 39.57 A C ANISOU 2109 CA ALA A 293 3736 6786 4512 -610 254 494 A C ATOM 2110 C ALA A 293 -50.972 26.645 55.713 1.00 40.17 A C ANISOU 2110 C ALA A 293 3849 6611 4802 -692 84 477 A C ATOM 2111 O ALA A 293 -51.699 27.577 55.349 1.00 40.65 A O ANISOU 2111 O ALA A 293 4027 6639 4778 -594 32 334 A O ATOM 2112 CB ALA A 293 -51.207 25.727 58.040 1.00 36.78 A C ANISOU 2112 CB ALA A 293 3535 6446 3993 -505 18 424 A C ATOM 2113 N ALA A 294 -49.677 26.588 55.392 1.00 36.81 A N ANISOU 2113 N ALA A 294 3320 6007 4658 -872 -10 629 A N ATOM 2114 CA ALA A 294 -49.096 27.602 54.518 1.00 40.21 A C ANISOU 2114 CA ALA A 294 3760 6208 5312 -983 -150 655 A C ATOM 2115 C ALA A 294 -49.794 27.614 53.165 1.00 45.56 A C ANISOU 2115 C ALA A 294 4386 6901 6022 -1006 89 659 A C ATOM 2116 O ALA A 294 -49.992 28.677 52.566 1.00 50.64 A O ANISOU 2116 O ALA A 294 5134 7407 6701 -1006 -23 585 A O ATOM 2117 CB ALA A 294 -47.596 27.365 54.349 1.00 36.04 A C ANISOU 2117 CB ALA A 294 3071 5527 5094 -1182 -236 855 A C ATOM 2118 N LEU A 295 -50.167 26.435 52.664 1.00 41.91 A N ANISOU 2118 N LEU A 295 3783 6591 5551 -1025 397 747 A N ATOM 2119 CA LEU A 295 -50.806 26.353 51.356 1.00 40.45 A C ANISOU 2119 CA LEU A 295 3561 6407 5400 -1044 616 759 A C ATOM 2120 C LEU A 295 -52.195 26.979 51.380 1.00 40.19 A C ANISOU 2120 C LEU A 295 3677 6455 5139 -875 612 558 A C ATOM 2121 O LEU A 295 -52.604 27.636 50.415 1.00 37.81 A O ANISOU 2121 O LEU A 295 3434 6055 4877 -878 627 507 A O ATOM 2122 CB LEU A 295 -50.881 24.892 50.912 1.00 39.64 A C ANISOU 2122 CB LEU A 295 3457 6276 5327 -994 848 791 A C ATOM 2123 CG LEU A 295 -51.173 24.597 49.443 1.00 34.42 A C ANISOU 2123 CG LEU A 295 2950 5378 4751 -932 981 694 A C ATOM 2124 CD1 LEU A 295 -50.002 25.049 48.582 1.00 35.72 A C ANISOU 2124 CD1 LEU A 295 3113 5369 5091 -1036 942 737 A C ATOM 2125 CD2 LEU A 295 -51.447 23.117 49.251 1.00 31.81 A C ANISOU 2125 CD2 LEU A 295 2747 4945 4394 -840 1088 601 A C ATOM 2126 N ARG A 296 -52.932 26.794 52.479 1.00 41.80 A N ANISOU 2126 N ARG A 296 3941 6841 5098 -720 593 444 A N ATOM 2127 CA ARG A 296 -54.295 27.312 52.549 1.00 40.27 A C ANISOU 2127 CA ARG A 296 3856 6764 4681 -535 614 257 A C ATOM 2128 C ARG A 296 -54.315 28.831 52.434 1.00 47.93 A C ANISOU 2128 C ARG A 296 5015 7552 5644 -466 349 102 A C ATOM 2129 O ARG A 296 -55.234 29.404 51.837 1.00 52.94 A O ANISOU 2129 O ARG A 296 5722 8184 6207 -373 371 -22 A O ATOM 2130 CB ARG A 296 -54.967 26.865 53.848 1.00 34.63 A C ANISOU 2130 CB ARG A 296 3166 6295 3698 -375 643 183 A C ATOM 2131 CG ARG A 296 -55.152 25.361 53.984 1.00 36.40 A C ANISOU 2131 CG ARG A 296 3222 6711 3898 -437 897 331 A C ATOM 2132 CD ARG A 296 -55.868 25.020 55.284 1.00 40.74 A C ANISOU 2132 CD ARG A 296 3806 7511 4161 -280 926 266 A C ATOM 2133 NE ARG A 296 -56.081 23.582 55.424 1.00 45.76 A N ANISOU 2133 NE ARG A 296 4368 8199 4821 -339 1089 401 A N ATOM 2134 CZ ARG A 296 -55.236 22.757 56.032 1.00 51.60 A C ANISOU 2134 CZ ARG A 296 5079 8920 5608 -426 1062 520 A C ATOM 2135 NH1 ARG A 296 -54.117 23.227 56.567 1.00 57.22 A N1+ ANISOU 2135 NH1 ARG A 296 5781 9617 6343 -482 906 547 A N1+ ATOM 2136 NH2 ARG A 296 -55.509 21.461 56.109 1.00 49.73 A N ANISOU 2136 NH2 ARG A 296 4917 8519 5458 -433 1097 573 A N ATOM 2137 N ARG A 297 -53.312 29.499 52.993 1.00 45.06 A N ANISOU 2137 N ARG A 297 4740 7020 5361 -514 72 108 A N ATOM 2138 CA ARG A 297 -53.224 30.949 52.922 1.00 46.67 A C ANISOU 2138 CA ARG A 297 5142 7017 5572 -467 -231 -24 A C ATOM 2139 C ARG A 297 -52.416 31.439 51.726 1.00 47.76 A C ANISOU 2139 C ARG A 297 5245 6907 5995 -679 -282 102 A C ATOM 2140 O ARG A 297 -52.222 32.651 51.585 1.00 51.67 A O ANISOU 2140 O ARG A 297 5904 7196 6531 -683 -557 25 A O ATOM 2141 CB ARG A 297 -52.630 31.507 54.223 1.00 50.11 A C ANISOU 2141 CB ARG A 297 5729 7382 5929 -394 -556 -94 A C ATOM 2142 CG ARG A 297 -51.178 31.126 54.476 1.00 51.42 A C ANISOU 2142 CG ARG A 297 5786 7421 6331 -598 -658 101 A C ATOM 2143 CD ARG A 297 -50.650 31.790 55.745 1.00 52.94 A C ANISOU 2143 CD ARG A 297 6166 7506 6442 -514 -1031 16 A C ATOM 2144 NE ARG A 297 -49.330 31.299 56.133 1.00 52.89 A N ANISOU 2144 NE ARG A 297 6040 7407 6650 -691 -1129 199 A N ATOM 2145 CZ ARG A 297 -49.125 30.376 57.067 1.00 53.05 A C ANISOU 2145 CZ ARG A 297 6009 7567 6582 -654 -1070 241 A C ATOM 2146 NH1 ARG A 297 -50.154 29.852 57.719 1.00 54.25 A N1+ ANISOU 2146 NH1 ARG A 297 6217 7967 6427 -457 -903 127 A N1+ ATOM 2147 NH2 ARG A 297 -47.894 29.984 57.361 1.00 54.47 A N ANISOU 2147 NH2 ARG A 297 6077 7641 6980 -814 -1183 403 A N ATOM 2148 N GLY A 298 -51.940 30.536 50.868 1.00 42.92 A N ANISOU 2148 N GLY A 298 4431 6306 5569 -849 -31 299 A N ATOM 2149 CA GLY A 298 -51.213 30.940 49.679 1.00 41.62 A C ANISOU 2149 CA GLY A 298 4223 5938 5654 -1038 -31 435 A C ATOM 2150 C GLY A 298 -49.796 31.393 49.933 1.00 46.47 A C ANISOU 2150 C GLY A 298 4799 6365 6493 -1208 -263 574 A C ATOM 2151 O GLY A 298 -49.212 32.076 49.086 1.00 49.33 A O ANISOU 2151 O GLY A 298 5164 6534 7044 -1358 -341 670 A O ATOM 2152 N ASP A 299 -49.226 31.034 51.082 1.00 49.10 A N ANISOU 2152 N ASP A 299 5097 6747 6814 -1195 -385 597 A N ATOM 2153 CA ASP A 299 -47.873 31.435 51.468 1.00 51.00 A C ANISOU 2153 CA ASP A 299 5291 6808 7278 -1352 -644 728 A C ATOM 2154 C ASP A 299 -46.863 30.481 50.834 1.00 51.97 A C ANISOU 2154 C ASP A 299 5137 6952 7658 -1538 -418 983 A C ATOM 2155 O ASP A 299 -46.321 29.575 51.471 1.00 53.82 A O ANISOU 2155 O ASP A 299 5239 7280 7930 -1553 -368 1067 A O ATOM 2156 CB ASP A 299 -47.753 31.468 52.986 1.00 52.92 A C ANISOU 2156 CB ASP A 299 5642 7083 7380 -1235 -890 628 A C ATOM 2157 CG ASP A 299 -46.504 32.177 53.459 1.00 56.78 A C ANISOU 2157 CG ASP A 299 6150 7341 8083 -1374 -1258 720 A C ATOM 2158 OD1 ASP A 299 -45.583 32.373 52.639 1.00 57.09 A O ANISOU 2158 OD1 ASP A 299 6038 7238 8414 -1591 -1263 914 A O ATOM 2159 OD2 ASP A 299 -46.447 32.540 54.654 1.00 59.20 A O1- ANISOU 2159 OD2 ASP A 299 6624 7606 8262 -1264 -1548 606 A O1- ATOM 2160 N TYR A 300 -46.606 30.698 49.542 1.00 49.19 A N ANISOU 2160 N TYR A 300 4707 6510 7474 -1670 -282 1105 A N ATOM 2161 CA TYR A 300 -45.709 29.808 48.811 1.00 45.90 A C ANISOU 2161 CA TYR A 300 4120 6112 7208 -1727 -25 1266 A C ATOM 2162 C TYR A 300 -44.274 29.918 49.315 1.00 45.34 A C ANISOU 2162 C TYR A 300 3974 5936 7319 -1804 -207 1375 A C ATOM 2163 O TYR A 300 -43.551 28.916 49.364 1.00 43.12 A O ANISOU 2163 O TYR A 300 3634 5717 7033 -1725 -53 1392 A O ATOM 2164 CB TYR A 300 -45.781 30.103 47.314 1.00 45.34 A C ANISOU 2164 CB TYR A 300 4149 5954 7125 -1698 159 1237 A C ATOM 2165 CG TYR A 300 -47.170 29.959 46.742 1.00 40.07 A C ANISOU 2165 CG TYR A 300 3565 5367 6291 -1612 333 1127 A C ATOM 2166 CD1 TYR A 300 -48.070 29.046 47.281 1.00 40.02 A C ANISOU 2166 CD1 TYR A 300 3542 5548 6116 -1491 470 1042 A C ATOM 2167 CD2 TYR A 300 -47.577 30.721 45.657 1.00 38.46 A C ANISOU 2167 CD2 TYR A 300 3465 5054 6093 -1647 359 1111 A C ATOM 2168 CE1 TYR A 300 -49.339 28.905 46.762 1.00 38.04 A C ANISOU 2168 CE1 TYR A 300 3363 5377 5712 -1398 623 941 A C ATOM 2169 CE2 TYR A 300 -48.844 30.585 45.129 1.00 38.44 A C ANISOU 2169 CE2 TYR A 300 3535 5119 5951 -1567 504 1015 A C ATOM 2170 CZ TYR A 300 -49.720 29.678 45.685 1.00 38.52 A C ANISOU 2170 CZ TYR A 300 3514 5324 5800 -1438 637 929 A C ATOM 2171 OH TYR A 300 -50.981 29.551 45.153 1.00 39.32 A O ANISOU 2171 OH TYR A 300 3682 5498 5760 -1345 774 832 A O ATOM 2172 N ARG A 301 -43.838 31.124 49.686 1.00 51.16 A N ANISOU 2172 N ARG A 301 4736 6492 8212 -1956 -570 1433 A N ATOM 2173 CA ARG A 301 -42.496 31.276 50.242 1.00 53.99 A C ANISOU 2173 CA ARG A 301 5024 6743 8747 -2023 -775 1541 A C ATOM 2174 C ARG A 301 -42.315 30.411 51.481 1.00 51.75 A C ANISOU 2174 C ARG A 301 4657 6564 8441 -1989 -845 1540 A C ATOM 2175 O ARG A 301 -41.289 29.738 51.637 1.00 53.56 A O ANISOU 2175 O ARG A 301 4790 6810 8750 -1958 -772 1617 A O ATOM 2176 CB ARG A 301 -42.218 32.740 50.582 1.00 64.49 A C ANISOU 2176 CB ARG A 301 6459 7829 10213 -2170 -1225 1563 A C ATOM 2177 CG ARG A 301 -42.180 33.680 49.391 1.00 72.68 A C ANISOU 2177 CG ARG A 301 7582 8739 11294 -2225 -1195 1597 A C ATOM 2178 CD ARG A 301 -41.621 35.037 49.798 1.00 81.03 A C ANISOU 2178 CD ARG A 301 8760 9537 12492 -2352 -1661 1636 A C ATOM 2179 NE ARG A 301 -42.114 35.470 51.104 1.00 88.33 A N ANISOU 2179 NE ARG A 301 9839 10359 13362 -2359 -2104 1488 A N ATOM 2180 CZ ARG A 301 -41.442 35.317 52.241 1.00 93.07 A C ANISOU 2180 CZ ARG A 301 10420 10917 14026 -2359 -2360 1504 A C ATOM 2181 NH1 ARG A 301 -40.246 34.745 52.229 1.00 95.37 A N1+ ANISOU 2181 NH1 ARG A 301 10516 11250 14469 -2379 -2210 1684 A N1+ ATOM 2182 NH2 ARG A 301 -41.961 35.738 53.388 1.00 93.32 A N ANISOU 2182 NH2 ARG A 301 10727 10897 13833 -2182 -2674 1279 A N ATOM 2183 N ALA A 302 -43.303 30.423 52.378 1.00 52.37 A N ANISOU 2183 N ALA A 302 4852 6722 8323 -1906 -972 1390 A N ATOM 2184 CA ALA A 302 -43.238 29.581 53.568 1.00 53.81 A C ANISOU 2184 CA ALA A 302 5032 7023 8389 -1804 -1007 1343 A C ATOM 2185 C ALA A 302 -43.273 28.104 53.201 1.00 50.95 A C ANISOU 2185 C ALA A 302 4465 6868 8027 -1793 -621 1441 A C ATOM 2186 O ALA A 302 -42.542 27.295 53.784 1.00 53.78 A O ANISOU 2186 O ALA A 302 4729 7260 8445 -1789 -621 1510 A O ATOM 2187 CB ALA A 302 -44.386 29.923 54.517 1.00 41.53 A C ANISOU 2187 CB ALA A 302 3765 5536 6478 -1577 -1133 1083 A C ATOM 2188 N PHE A 303 -44.128 27.732 52.249 1.00 45.57 A N ANISOU 2188 N PHE A 303 3808 6291 7214 -1712 -297 1389 A N ATOM 2189 CA PHE A 303 -44.184 26.344 51.807 1.00 35.89 A C ANISOU 2189 CA PHE A 303 2606 5170 5861 -1552 47 1333 A C ATOM 2190 C PHE A 303 -42.836 25.893 51.256 1.00 41.32 A C ANISOU 2190 C PHE A 303 3267 5755 6676 -1536 111 1381 A C ATOM 2191 O PHE A 303 -42.365 24.793 51.570 1.00 41.26 A O ANISOU 2191 O PHE A 303 3233 5800 6645 -1471 190 1381 A O ATOM 2192 CB PHE A 303 -45.289 26.193 50.761 1.00 33.97 A C ANISOU 2192 CB PHE A 303 2479 4973 5456 -1447 301 1211 A C ATOM 2193 CG PHE A 303 -45.691 24.770 50.487 1.00 32.20 A C ANISOU 2193 CG PHE A 303 2341 4820 5073 -1294 547 1099 A C ATOM 2194 CD1 PHE A 303 -44.933 23.961 49.660 1.00 34.42 A C ANISOU 2194 CD1 PHE A 303 2675 5029 5374 -1244 667 1058 A C ATOM 2195 CD2 PHE A 303 -46.847 24.250 51.046 1.00 34.81 A C ANISOU 2195 CD2 PHE A 303 2706 5296 5225 -1212 622 1033 A C ATOM 2196 CE1 PHE A 303 -45.316 22.656 49.406 1.00 32.50 A C ANISOU 2196 CE1 PHE A 303 2531 4819 5000 -1140 811 947 A C ATOM 2197 CE2 PHE A 303 -47.234 22.949 50.794 1.00 33.08 A C ANISOU 2197 CE2 PHE A 303 2597 5077 4895 -1094 786 926 A C ATOM 2198 CZ PHE A 303 -46.469 22.152 49.972 1.00 30.93 A C ANISOU 2198 CZ PHE A 303 2387 4700 4667 -1072 860 879 A C ATOM 2199 N GLY A 304 -42.193 26.737 50.445 1.00 41.01 A N ANISOU 2199 N GLY A 304 3228 5587 6767 -1603 66 1432 A N ATOM 2200 CA GLY A 304 -40.876 26.399 49.926 1.00 41.58 A C ANISOU 2200 CA GLY A 304 3238 5608 6952 -1600 119 1500 A C ATOM 2201 C GLY A 304 -39.840 26.179 51.013 1.00 47.57 A C ANISOU 2201 C GLY A 304 3873 6340 7863 -1653 -80 1611 A C ATOM 2202 O GLY A 304 -39.009 25.273 50.916 1.00 47.26 A O ANISOU 2202 O GLY A 304 3772 6332 7852 -1599 15 1638 A O ATOM 2203 N ARG A 305 -39.871 27.003 52.062 1.00 49.81 A N ANISOU 2203 N ARG A 305 4130 6549 8247 -1765 -395 1668 A N ATOM 2204 CA ARG A 305 -38.900 26.843 53.142 1.00 47.15 A C ANISOU 2204 CA ARG A 305 3699 6156 8060 -1822 -637 1762 A C ATOM 2205 C ARG A 305 -39.092 25.517 53.866 1.00 44.94 A C ANISOU 2205 C ARG A 305 3394 6015 7668 -1734 -534 1727 A C ATOM 2206 O ARG A 305 -38.116 24.826 54.181 1.00 43.36 A O ANISOU 2206 O ARG A 305 3108 5806 7561 -1718 -549 1792 A O ATOM 2207 CB ARG A 305 -38.999 28.013 54.122 1.00 50.36 A C ANISOU 2207 CB ARG A 305 4148 6420 8566 -1955 -1071 1783 A C ATOM 2208 CG ARG A 305 -38.289 29.276 53.670 1.00 53.56 A C ANISOU 2208 CG ARG A 305 4571 6627 9152 -2062 -1277 1865 A C ATOM 2209 CD ARG A 305 -38.415 30.394 54.701 1.00 59.66 A C ANISOU 2209 CD ARG A 305 5467 7212 9988 -2166 -1781 1833 A C ATOM 2210 NE ARG A 305 -39.671 31.133 54.575 1.00 66.08 A N ANISOU 2210 NE ARG A 305 6435 8012 10659 -2178 -1882 1697 A N ATOM 2211 CZ ARG A 305 -40.723 31.014 55.381 1.00 70.94 A C ANISOU 2211 CZ ARG A 305 7224 8719 11009 -2047 -1966 1503 A C ATOM 2212 NH1 ARG A 305 -40.709 30.169 56.404 1.00 72.75 A N1+ ANISOU 2212 NH1 ARG A 305 7473 9058 11112 -1937 -1973 1451 A N1+ ATOM 2213 NH2 ARG A 305 -41.801 31.754 55.155 1.00 71.03 A N ANISOU 2213 NH2 ARG A 305 7475 8723 10789 -1925 -1978 1319 A N ATOM 2214 N LEU A 306 -40.343 25.138 54.129 1.00 40.68 A N ANISOU 2214 N LEU A 306 2921 5609 6926 -1679 -432 1633 A N ATOM 2215 CA LEU A 306 -40.596 23.843 54.747 1.00 44.93 A C ANISOU 2215 CA LEU A 306 3449 6286 7335 -1596 -316 1607 A C ATOM 2216 C LEU A 306 -40.139 22.705 53.845 1.00 45.56 A C ANISOU 2216 C LEU A 306 3549 6386 7375 -1477 -35 1569 A C ATOM 2217 O LEU A 306 -39.676 21.668 54.334 1.00 46.73 A O ANISOU 2217 O LEU A 306 3659 6574 7523 -1438 -20 1595 A O ATOM 2218 CB LEU A 306 -42.082 23.710 55.082 1.00 38.11 A C ANISOU 2218 CB LEU A 306 2650 5591 6240 -1556 -233 1526 A C ATOM 2219 CG LEU A 306 -42.620 24.744 56.077 1.00 39.30 A C ANISOU 2219 CG LEU A 306 2849 5753 6332 -1622 -553 1492 A C ATOM 2220 CD1 LEU A 306 -44.140 24.778 56.063 1.00 40.48 A C ANISOU 2220 CD1 LEU A 306 3180 6055 6145 -1464 -389 1317 A C ATOM 2221 CD2 LEU A 306 -42.092 24.487 57.487 1.00 49.49 A C ANISOU 2221 CD2 LEU A 306 4215 7013 7577 -1586 -820 1471 A C ATOM 2222 N MET A 307 -40.259 22.882 52.527 1.00 45.67 A N ANISOU 2222 N MET A 307 3631 6369 7352 -1430 150 1504 A N ATOM 2223 CA MET A 307 -39.762 21.877 51.594 1.00 44.44 A C ANISOU 2223 CA MET A 307 3504 6223 7158 -1338 349 1459 A C ATOM 2224 C MET A 307 -38.251 21.717 51.701 1.00 44.74 A C ANISOU 2224 C MET A 307 3400 6209 7390 -1374 262 1585 A C ATOM 2225 O MET A 307 -37.732 20.596 51.640 1.00 48.66 A O ANISOU 2225 O MET A 307 3871 6742 7877 -1308 341 1588 A O ATOM 2226 CB MET A 307 -40.155 22.252 50.167 1.00 46.00 A C ANISOU 2226 CB MET A 307 3803 6395 7281 -1307 509 1374 A C ATOM 2227 CG MET A 307 -41.643 22.171 49.884 1.00 40.45 A C ANISOU 2227 CG MET A 307 3250 5737 6384 -1249 621 1232 A C ATOM 2228 SD MET A 307 -42.019 22.792 48.239 1.00 41.19 A S ANISOU 2228 SD MET A 307 3442 5779 6429 -1238 745 1177 A S ATOM 2229 CE MET A 307 -41.073 21.653 47.230 1.00 40.38 A C ANISOU 2229 CE MET A 307 3278 5684 6380 -1151 847 1298 A C ATOM 2230 N VAL A 308 -37.524 22.827 51.850 1.00 44.10 A N ANISOU 2230 N VAL A 308 3224 6033 7498 -1482 84 1698 A N ATOM 2231 CA VAL A 308 -36.068 22.743 51.900 1.00 46.32 A C ANISOU 2231 CA VAL A 308 3356 6260 7982 -1519 -1 1829 A C ATOM 2232 C VAL A 308 -35.612 22.143 53.221 1.00 47.64 A C ANISOU 2232 C VAL A 308 3443 6427 8230 -1536 -176 1891 A C ATOM 2233 O VAL A 308 -34.632 21.388 53.271 1.00 48.02 A O ANISOU 2233 O VAL A 308 3389 6481 8375 -1506 -161 1957 A O ATOM 2234 CB VAL A 308 -35.434 24.125 51.663 1.00 49.13 A C ANISOU 2234 CB VAL A 308 3643 6498 8526 -1640 -165 1939 A C ATOM 2235 CG1 VAL A 308 -33.919 24.007 51.666 1.00 48.04 A C ANISOU 2235 CG1 VAL A 308 3334 6313 8605 -1676 -238 2085 A C ATOM 2236 CG2 VAL A 308 -35.919 24.717 50.350 1.00 47.71 A C ANISOU 2236 CG2 VAL A 308 3549 6320 8259 -1631 4 1883 A C ATOM 2237 N GLU A 309 -36.310 22.468 54.312 1.00 48.68 A N ANISOU 2237 N GLU A 309 3616 6555 8324 -1587 -359 1876 A N ATOM 2238 CA GLU A 309 -36.021 21.825 55.588 1.00 48.90 A C ANISOU 2238 CA GLU A 309 3594 6593 8393 -1604 -533 1921 A C ATOM 2239 C GLU A 309 -36.236 20.322 55.495 1.00 49.80 A C ANISOU 2239 C GLU A 309 3733 6826 8364 -1488 -315 1868 A C ATOM 2240 O GLU A 309 -35.423 19.536 55.996 1.00 50.53 A O ANISOU 2240 O GLU A 309 3740 6910 8547 -1476 -379 1934 A O ATOM 2241 CB GLU A 309 -36.899 22.420 56.688 1.00 48.82 A C ANISOU 2241 CB GLU A 309 3647 6584 8318 -1677 -771 1894 A C ATOM 2242 CG GLU A 309 -36.663 23.895 56.961 1.00 56.17 A C ANISOU 2242 CG GLU A 309 4590 7355 9398 -1800 -1088 1933 A C ATOM 2243 CD GLU A 309 -37.651 24.460 57.967 1.00 63.81 A C ANISOU 2243 CD GLU A 309 5655 8336 10254 -1856 -1359 1863 A C ATOM 2244 OE1 GLU A 309 -38.132 23.683 58.822 1.00 65.60 A O ANISOU 2244 OE1 GLU A 309 5894 8689 10344 -1827 -1389 1833 A O ATOM 2245 OE2 GLU A 309 -37.955 25.671 57.899 1.00 65.87 A O1- ANISOU 2245 OE2 GLU A 309 5993 8490 10544 -1925 -1565 1830 A O1- ATOM 2246 N SER A 310 -37.330 19.903 54.855 1.00 49.38 A N ANISOU 2246 N SER A 310 3804 6865 8093 -1403 -81 1748 A N ATOM 2247 CA SER A 310 -37.587 18.479 54.675 1.00 46.14 A C ANISOU 2247 CA SER A 310 3450 6536 7544 -1297 97 1690 A C ATOM 2248 C SER A 310 -36.416 17.792 53.983 1.00 46.66 A C ANISOU 2248 C SER A 310 3436 6571 7721 -1248 172 1735 A C ATOM 2249 O SER A 310 -36.006 16.696 54.384 1.00 47.03 A O ANISOU 2249 O SER A 310 3443 6646 7781 -1208 169 1770 A O ATOM 2250 CB SER A 310 -38.875 18.278 53.878 1.00 44.27 A C ANISOU 2250 CB SER A 310 3379 6357 7086 -1219 306 1543 A C ATOM 2251 OG SER A 310 -39.090 16.906 53.606 1.00 44.86 A O ANISOU 2251 OG SER A 310 3525 6475 7045 -1126 440 1485 A O ATOM 2252 N HIS A 311 -35.869 18.417 52.938 1.00 46.47 A N ANISOU 2252 N HIS A 311 3380 6498 7778 -1255 237 1747 A N ATOM 2253 CA HIS A 311 -34.739 17.819 52.233 1.00 45.75 A C ANISOU 2253 CA HIS A 311 3190 6401 7792 -1211 316 1808 A C ATOM 2254 C HIS A 311 -33.524 17.712 53.149 1.00 51.48 A C ANISOU 2254 C HIS A 311 3737 7083 8742 -1263 129 1953 A C ATOM 2255 O HIS A 311 -32.869 16.664 53.208 1.00 53.39 A O ANISOU 2255 O HIS A 311 3904 7349 9032 -1207 159 1995 A O ATOM 2256 CB HIS A 311 -34.406 18.622 50.975 1.00 45.38 A C ANISOU 2256 CB HIS A 311 3128 6324 7790 -1225 411 1822 A C ATOM 2257 CG HIS A 311 -33.309 18.019 50.153 1.00 44.53 A C ANISOU 2257 CG HIS A 311 2883 6227 7811 -1166 503 1950 A C ATOM 2258 CD2 HIS A 311 -32.025 18.401 49.959 1.00 48.54 A C ANISOU 2258 CD2 HIS A 311 3209 6702 8531 -1212 457 2088 A C ATOM 2259 ND1 HIS A 311 -33.482 16.869 49.413 1.00 43.88 A N ANISOU 2259 ND1 HIS A 311 2838 6193 7643 -1044 660 1949 A N ATOM 2260 CE1 HIS A 311 -32.353 16.570 48.797 1.00 45.93 A C ANISOU 2260 CE1 HIS A 311 2945 6459 8050 -1009 720 2072 A C ATOM 2261 NE2 HIS A 311 -31.452 17.483 49.112 1.00 50.14 A N ANISOU 2261 NE2 HIS A 311 3336 6949 8766 -1111 606 2162 A N ATOM 2262 N ARG A 312 -33.198 18.795 53.862 1.00 53.32 A N ANISOU 2262 N ARG A 312 3900 7234 9126 -1375 -91 2033 A N ATOM 2263 CA ARG A 312 -32.100 18.740 54.824 1.00 56.03 A C ANISOU 2263 CA ARG A 312 4092 7506 9691 -1436 -321 2160 A C ATOM 2264 C ARG A 312 -32.301 17.592 55.806 1.00 55.94 A C ANISOU 2264 C ARG A 312 4097 7539 9618 -1397 -377 2146 A C ATOM 2265 O ARG A 312 -31.374 16.824 56.085 1.00 57.46 A O ANISOU 2265 O ARG A 312 4174 7719 9937 -1374 -425 2220 A O ATOM 2266 CB ARG A 312 -31.980 20.066 55.584 1.00 58.34 A C ANISOU 2266 CB ARG A 312 4365 7679 10124 -1568 -609 2223 A C ATOM 2267 CG ARG A 312 -31.653 21.286 54.736 1.00 61.33 A C ANISOU 2267 CG ARG A 312 4711 7990 10602 -1632 -609 2273 A C ATOM 2268 CD ARG A 312 -31.420 22.511 55.617 1.00 64.26 A C ANISOU 2268 CD ARG A 312 5073 8206 11137 -1768 -963 2348 A C ATOM 2269 NE ARG A 312 -31.534 23.755 54.861 1.00 65.39 A N ANISOU 2269 NE ARG A 312 5242 8288 11317 -1836 -972 2371 A N ATOM 2270 CZ ARG A 312 -30.543 24.307 54.168 1.00 67.53 A C ANISOU 2270 CZ ARG A 312 5390 8504 11763 -1887 -971 2491 A C ATOM 2271 NH1 ARG A 312 -29.350 23.727 54.134 1.00 72.16 A N1+ ANISOU 2271 NH1 ARG A 312 5809 9095 12513 -1873 -956 2598 A N1+ ATOM 2272 NH2 ARG A 312 -30.747 25.441 53.507 1.00 62.46 A N ANISOU 2272 NH2 ARG A 312 4787 7806 11139 -1958 -990 2514 A N ATOM 2273 N SER A 313 -33.515 17.471 56.350 1.00 53.79 A N ANISOU 2273 N SER A 313 3958 7324 9155 -1394 -378 2062 A N ATOM 2274 CA SER A 313 -33.819 16.379 57.269 1.00 54.63 A C ANISOU 2274 CA SER A 313 4090 7490 9178 -1369 -426 2060 A C ATOM 2275 C SER A 313 -33.641 15.025 56.592 1.00 56.55 A C ANISOU 2275 C SER A 313 4334 7798 9355 -1255 -215 2039 A C ATOM 2276 O SER A 313 -33.014 14.117 57.149 1.00 57.70 A O ANISOU 2276 O SER A 313 4402 7941 9581 -1240 -295 2105 A O ATOM 2277 CB SER A 313 -35.242 16.532 57.809 1.00 54.79 A C ANISOU 2277 CB SER A 313 4246 7593 8980 -1387 -425 1985 A C ATOM 2278 OG SER A 313 -35.558 15.495 58.722 1.00 57.89 A O ANISOU 2278 OG SER A 313 4659 8060 9277 -1380 -477 2006 A O ATOM 2279 N LEU A 314 -34.184 14.873 55.381 1.00 53.11 A N ANISOU 2279 N LEU A 314 3995 7406 8777 -1176 26 1946 A N ATOM 2280 CA LEU A 314 -34.068 13.599 54.677 1.00 50.44 A C ANISOU 2280 CA LEU A 314 3679 7112 8372 -1070 192 1921 A C ATOM 2281 C LEU A 314 -32.625 13.282 54.313 1.00 51.12 A C ANISOU 2281 C LEU A 314 3590 7165 8668 -1045 181 2024 A C ATOM 2282 O LEU A 314 -32.260 12.107 54.204 1.00 51.46 A O ANISOU 2282 O LEU A 314 3595 7235 8721 -972 230 2053 A O ATOM 2283 CB LEU A 314 -34.940 13.599 53.420 1.00 42.89 A C ANISOU 2283 CB LEU A 314 2878 6185 7234 -1002 404 1793 A C ATOM 2284 CG LEU A 314 -36.457 13.495 53.596 1.00 40.04 A C ANISOU 2284 CG LEU A 314 2701 5869 6645 -991 460 1676 A C ATOM 2285 CD1 LEU A 314 -37.167 13.923 52.320 1.00 36.69 A C ANISOU 2285 CD1 LEU A 314 2395 5434 6112 -948 609 1582 A C ATOM 2286 CD2 LEU A 314 -36.859 12.078 53.975 1.00 37.27 A C ANISOU 2286 CD2 LEU A 314 2406 5565 6189 -936 485 1676 A C ATOM 2287 N ARG A 315 -31.795 14.305 54.117 1.00 52.86 A N ANISOU 2287 N ARG A 315 3693 7326 9065 -1107 112 2092 A N ATOM 2288 CA ARG A 315 -30.417 14.069 53.705 1.00 57.80 A C ANISOU 2288 CA ARG A 315 4133 7933 9896 -1086 118 2201 A C ATOM 2289 C ARG A 315 -29.515 13.763 54.893 1.00 60.95 A C ANISOU 2289 C ARG A 315 4384 8279 10497 -1132 -108 2309 A C ATOM 2290 O ARG A 315 -28.591 12.951 54.780 1.00 63.27 A O ANISOU 2290 O ARG A 315 4541 8582 10915 -1077 -92 2379 A O ATOM 2291 CB ARG A 315 -29.888 15.285 52.954 1.00 55.21 A C ANISOU 2291 CB ARG A 315 3732 7567 9679 -1143 139 2247 A C ATOM 2292 CG ARG A 315 -28.489 15.137 52.418 1.00 56.62 A C ANISOU 2292 CG ARG A 315 3703 7745 10068 -1126 172 2372 A C ATOM 2293 CD ARG A 315 -28.000 16.487 51.966 1.00 55.71 A C ANISOU 2293 CD ARG A 315 3506 7579 10083 -1220 135 2447 A C ATOM 2294 NE ARG A 315 -27.834 17.383 53.108 1.00 55.17 A N ANISOU 2294 NE ARG A 315 3399 7405 10158 -1344 -141 2509 A N ATOM 2295 CZ ARG A 315 -27.924 18.707 53.049 1.00 65.63 A C ANISOU 2295 CZ ARG A 315 4735 8658 11542 -1448 -242 2542 A C ATOM 2296 NH1 ARG A 315 -28.070 19.313 51.878 1.00 67.71 A N1+ ANISOU 2296 NH1 ARG A 315 5024 8952 11750 -1450 -78 2532 A N1+ ATOM 2297 NH2 ARG A 315 -27.764 19.429 54.151 1.00 68.40 A N ANISOU 2297 NH2 ARG A 315 5066 8894 12028 -1556 -532 2599 A N ATOM 2298 N ASP A 316 -29.756 14.407 56.034 1.00 59.84 A N ANISOU 2298 N ASP A 316 4266 8074 10396 -1230 -337 2323 A N ATOM 2299 CA ASP A 316 -28.851 14.307 57.172 1.00 58.62 A C ANISOU 2299 CA ASP A 316 3987 7834 10453 -1290 -607 2421 A C ATOM 2300 C ASP A 316 -29.301 13.288 58.209 1.00 57.56 A C ANISOU 2300 C ASP A 316 3917 7724 10231 -1275 -714 2399 A C ATOM 2301 O ASP A 316 -28.513 12.430 58.615 1.00 63.11 A O ANISOU 2301 O ASP A 316 4514 8406 11059 -1246 -800 2460 A O ATOM 2302 CB ASP A 316 -28.706 15.675 57.849 1.00 58.77 A C ANISOU 2302 CB ASP A 316 4000 7734 10596 -1418 -865 2461 A C ATOM 2303 CG ASP A 316 -28.151 16.732 56.919 1.00 58.93 A C ANISOU 2303 CG ASP A 316 3939 7716 10737 -1457 -803 2516 A C ATOM 2304 OD1 ASP A 316 -27.500 16.361 55.921 1.00 59.06 A O ANISOU 2304 OD1 ASP A 316 3847 7787 10805 -1394 -609 2555 A O ATOM 2305 OD2 ASP A 316 -28.361 17.933 57.191 1.00 57.03 A O1- ANISOU 2305 OD2 ASP A 316 3741 7390 10538 -1553 -963 2528 A O1- ATOM 2306 N ASP A 317 -30.556 13.363 58.646 1.00 59.20 A N ANISOU 2306 N ASP A 317 4572 7750 10169 -1466 -1743 3942 A N ATOM 2307 CA ASP A 317 -31.034 12.489 59.709 1.00 61.95 A C ANISOU 2307 CA ASP A 317 5016 8096 10427 -1575 -1951 4079 A C ATOM 2308 C ASP A 317 -31.521 11.141 59.187 1.00 61.13 A C ANISOU 2308 C ASP A 317 4874 7883 10470 -1438 -1882 4107 A C ATOM 2309 O ASP A 317 -31.175 10.096 59.748 1.00 61.45 A O ANISOU 2309 O ASP A 317 4860 7826 10660 -1468 -2035 4278 A O ATOM 2310 CB ASP A 317 -32.146 13.189 60.496 1.00 62.56 A C ANISOU 2310 CB ASP A 317 5336 8325 10108 -1746 -2016 3985 A C ATOM 2311 CG ASP A 317 -31.608 14.206 61.485 1.00 65.05 A C ANISOU 2311 CG ASP A 317 5714 8727 10274 -1940 -2173 4028 A C ATOM 2312 OD1 ASP A 317 -30.377 14.247 61.695 1.00 68.26 A O ANISOU 2312 OD1 ASP A 317 5976 9076 10884 -1958 -2272 4162 A O ATOM 2313 OD2 ASP A 317 -32.419 14.963 62.057 1.00 64.52 A O1- ANISOU 2313 OD2 ASP A 317 5841 8783 9890 -2079 -2194 3919 A O1- ATOM 2314 N TYR A 318 -32.322 11.142 58.123 1.00 59.04 A N ANISOU 2314 N TYR A 318 4644 7622 10167 -1299 -1656 3940 A N ATOM 2315 CA TYR A 318 -32.861 9.898 57.589 1.00 58.08 A C ANISOU 2315 CA TYR A 318 4501 7402 10167 -1173 -1580 3954 A C ATOM 2316 C TYR A 318 -31.949 9.248 56.560 1.00 59.46 A C ANISOU 2316 C TYR A 318 4469 7416 10709 -976 -1427 3974 A C ATOM 2317 O TYR A 318 -32.066 8.038 56.330 1.00 60.22 A O ANISOU 2317 O TYR A 318 4514 7394 10972 -889 -1411 4032 A O ATOM 2318 CB TYR A 318 -34.235 10.140 56.960 1.00 58.03 A C ANISOU 2318 CB TYR A 318 4641 7472 9936 -1125 -1414 3763 A C ATOM 2319 CG TYR A 318 -35.246 9.061 57.274 1.00 56.72 A C ANISOU 2319 CG TYR A 318 4564 7294 9691 -1146 -1478 3802 A C ATOM 2320 CD1 TYR A 318 -35.753 8.913 58.557 1.00 57.41 A C ANISOU 2320 CD1 TYR A 318 4788 7466 9560 -1343 -1696 3883 A C ATOM 2321 CD2 TYR A 318 -35.688 8.187 56.289 1.00 53.47 A C ANISOU 2321 CD2 TYR A 318 4111 6787 9417 -981 -1315 3755 A C ATOM 2322 CE1 TYR A 318 -36.680 7.931 58.850 1.00 57.83 A C ANISOU 2322 CE1 TYR A 318 4928 7514 9531 -1382 -1754 3917 A C ATOM 2323 CE2 TYR A 318 -36.611 7.199 56.574 1.00 54.13 A C ANISOU 2323 CE2 TYR A 318 4273 6861 9432 -1011 -1378 3793 A C ATOM 2324 CZ TYR A 318 -37.105 7.078 57.854 1.00 55.15 A C ANISOU 2324 CZ TYR A 318 4531 7081 9342 -1215 -1601 3874 A C ATOM 2325 OH TYR A 318 -38.023 6.096 58.141 1.00 53.84 A O ANISOU 2325 OH TYR A 318 4448 6910 9098 -1265 -1664 3911 A O ATOM 2326 N GLU A 319 -31.042 10.013 55.951 1.00 61.74 A N ANISOU 2326 N GLU A 319 4640 7695 11121 -916 -1307 3917 A N ATOM 2327 CA GLU A 319 -30.126 9.489 54.944 1.00 66.97 A C ANISOU 2327 CA GLU A 319 5108 8215 12122 -738 -1134 3909 A C ATOM 2328 C GLU A 319 -30.840 8.595 53.937 1.00 66.68 A C ANISOU 2328 C GLU A 319 5096 8087 12154 -574 -932 3823 A C ATOM 2329 O GLU A 319 -30.604 7.382 53.904 1.00 68.40 A O ANISOU 2329 O GLU A 319 5227 8173 12591 -496 -953 3907 A O ATOM 2330 CB GLU A 319 -28.992 8.714 55.619 1.00 71.84 A C ANISOU 2330 CB GLU A 319 5554 8723 13018 -758 -1316 4097 A C ATOM 2331 CG GLU A 319 -28.215 9.521 56.650 1.00 74.07 A C ANISOU 2331 CG GLU A 319 5807 9083 13252 -927 -1532 4201 A C ATOM 2332 CD GLU A 319 -27.114 8.717 57.317 1.00 78.99 A C ANISOU 2332 CD GLU A 319 6259 9590 14163 -949 -1726 4389 A C ATOM 2333 OE1 GLU A 319 -27.213 7.473 57.353 1.00 80.40 A O ANISOU 2333 OE1 GLU A 319 6397 9647 14503 -886 -1766 4460 A O ATOM 2334 OE2 GLU A 319 -26.146 9.334 57.806 1.00 83.32 A O1- ANISOU 2334 OE2 GLU A 319 6711 10167 14780 -1033 -1844 4461 A O1- ATOM 2335 N VAL A 320 -31.711 9.178 53.114 1.00 68.23 A N ANISOU 2335 N VAL A 320 5414 8345 12165 -526 -738 3650 A N ATOM 2336 CA VAL A 320 -32.375 8.428 52.054 1.00 71.50 A C ANISOU 2336 CA VAL A 320 5862 8672 12634 -371 -525 3556 A C ATOM 2337 C VAL A 320 -32.212 9.143 50.718 1.00 74.91 A C ANISOU 2337 C VAL A 320 6296 9087 13078 -269 -233 3384 A C ATOM 2338 O VAL A 320 -32.806 8.741 49.712 1.00 73.36 A O ANISOU 2338 O VAL A 320 6162 8828 12884 -151 -24 3278 A O ATOM 2339 CB VAL A 320 -33.863 8.210 52.383 1.00 68.95 A C ANISOU 2339 CB VAL A 320 5721 8429 12046 -428 -585 3518 A C ATOM 2340 CG1 VAL A 320 -34.002 7.301 53.594 1.00 71.38 A C ANISOU 2340 CG1 VAL A 320 6033 8728 12361 -531 -848 3691 A C ATOM 2341 CG2 VAL A 320 -34.553 9.543 52.632 1.00 68.88 A C ANISOU 2341 CG2 VAL A 320 5868 8588 11717 -551 -599 3400 A C ATOM 2342 N SER A 321 -31.409 10.202 50.697 1.00 76.72 A N ANISOU 2342 N SER A 321 6472 9371 13309 -327 -216 3357 A N ATOM 2343 CA SER A 321 -31.099 10.908 49.464 1.00 77.74 A C ANISOU 2343 CA SER A 321 6602 9477 13457 -259 54 3207 A C ATOM 2344 C SER A 321 -29.825 10.322 48.856 1.00 81.08 A C ANISOU 2344 C SER A 321 6822 9765 14220 -145 185 3235 A C ATOM 2345 O SER A 321 -29.331 9.275 49.284 1.00 85.26 A O ANISOU 2345 O SER A 321 7220 10200 14973 -96 82 3357 A O ATOM 2346 CB SER A 321 -30.982 12.409 49.719 1.00 75.23 A C ANISOU 2346 CB SER A 321 6352 9291 12942 -399 15 3148 A C ATOM 2347 OG SER A 321 -29.804 12.715 50.444 1.00 79.32 A O ANISOU 2347 OG SER A 321 6715 9829 13595 -478 -134 3259 A O ATOM 2348 N CYS A 322 -29.279 10.996 47.849 1.00 83.94 A N ANISOU 2348 N CYS A 322 7161 10111 14622 -113 417 3116 A N ATOM 2349 CA CYS A 322 -28.043 10.566 47.209 1.00 88.17 A C ANISOU 2349 CA CYS A 322 7504 10530 15468 -19 572 3112 A C ATOM 2350 C CYS A 322 -27.405 11.780 46.551 1.00 90.32 A C ANISOU 2350 C CYS A 322 7764 10856 15697 -79 736 3005 A C ATOM 2351 O CYS A 322 -28.038 12.839 46.438 1.00 89.76 A O ANISOU 2351 O CYS A 322 7860 10886 15357 -172 755 2924 A O ATOM 2352 CB CYS A 322 -28.296 9.451 46.180 1.00 91.69 A C ANISOU 2352 CB CYS A 322 7966 10824 16049 148 802 3038 A C ATOM 2353 SG CYS A 322 -29.233 9.961 44.722 1.00 92.65 A S ANISOU 2353 SG CYS A 322 8325 10939 15938 191 1123 2827 A S ATOM 2354 N PRO A 323 -26.148 11.664 46.113 1.00 92.52 A N ANISOU 2354 N PRO A 323 7847 11066 16239 -37 857 2998 A N ATOM 2355 CA PRO A 323 -25.471 12.832 45.521 1.00 92.63 A C ANISOU 2355 CA PRO A 323 7842 11138 16215 -117 1011 2902 A C ATOM 2356 C PRO A 323 -26.230 13.465 44.366 1.00 89.33 A C ANISOU 2356 C PRO A 323 7651 10727 15563 -121 1264 2731 A C ATOM 2357 O PRO A 323 -26.295 14.697 44.281 1.00 91.90 A O ANISOU 2357 O PRO A 323 8075 11148 15694 -247 1279 2674 A O ATOM 2358 CB PRO A 323 -24.127 12.249 45.062 1.00 94.69 A C ANISOU 2358 CB PRO A 323 7854 11294 16829 -35 1147 2904 A C ATOM 2359 CG PRO A 323 -23.896 11.088 45.972 1.00 95.83 A C ANISOU 2359 CG PRO A 323 7852 11366 17192 32 926 3061 A C ATOM 2360 CD PRO A 323 -25.255 10.497 46.214 1.00 94.06 A C ANISOU 2360 CD PRO A 323 7824 11131 16784 70 843 3081 A C ATOM 2361 N GLU A 324 -26.810 12.658 43.475 1.00 84.94 A N ANISOU 2361 N GLU A 324 7194 10064 15015 5 1459 2650 A N ATOM 2362 CA GLU A 324 -27.545 13.213 42.342 1.00 81.47 A C ANISOU 2362 CA GLU A 324 6993 9616 14346 -4 1694 2494 A C ATOM 2363 C GLU A 324 -28.708 14.085 42.805 1.00 75.85 A C ANISOU 2363 C GLU A 324 6494 9019 13307 -107 1547 2485 A C ATOM 2364 O GLU A 324 -28.870 15.220 42.342 1.00 72.68 A O ANISOU 2364 O GLU A 324 6236 8669 12710 -207 1633 2399 A O ATOM 2365 CB GLU A 324 -28.053 12.087 41.439 1.00 85.31 A C ANISOU 2365 CB GLU A 324 7564 9963 14888 146 1895 2421 A C ATOM 2366 CG GLU A 324 -26.969 11.317 40.696 1.00 91.08 A C ANISOU 2366 CG GLU A 324 8132 10560 15913 244 2113 2378 A C ATOM 2367 CD GLU A 324 -26.257 10.300 41.570 1.00 95.15 A C ANISOU 2367 CD GLU A 324 8393 11021 16739 317 1940 2517 A C ATOM 2368 OE1 GLU A 324 -26.452 10.326 42.804 1.00 95.33 A O ANISOU 2368 OE1 GLU A 324 8357 11122 16740 266 1638 2659 A O ATOM 2369 OE2 GLU A 324 -25.503 9.471 41.017 1.00 97.89 A O1- ANISOU 2369 OE2 GLU A 324 8610 11239 17346 418 2105 2482 A O1- ATOM 2370 N LEU A 325 -29.533 13.570 43.719 1.00 72.40 A N ANISOU 2370 N LEU A 325 6085 8617 12806 -92 1326 2572 A N ATOM 2371 CA LEU A 325 -30.665 14.349 44.214 1.00 65.37 A C ANISOU 2371 CA LEU A 325 5388 7835 11615 -191 1186 2553 A C ATOM 2372 C LEU A 325 -30.206 15.635 44.890 1.00 61.59 A C ANISOU 2372 C LEU A 325 4890 7473 11038 -353 1048 2576 A C ATOM 2373 O LEU A 325 -30.777 16.707 44.657 1.00 56.88 A O ANISOU 2373 O LEU A 325 4475 6931 10208 -445 1078 2493 A O ATOM 2374 CB LEU A 325 -31.503 13.504 45.171 1.00 63.63 A C ANISOU 2374 CB LEU A 325 5175 7640 11363 -164 970 2646 A C ATOM 2375 CG LEU A 325 -32.336 12.409 44.503 1.00 62.28 A C ANISOU 2375 CG LEU A 325 5091 7370 11203 -30 1098 2603 A C ATOM 2376 CD1 LEU A 325 -33.091 11.603 45.542 1.00 61.75 A C ANISOU 2376 CD1 LEU A 325 5018 7338 11108 -31 869 2706 A C ATOM 2377 CD2 LEU A 325 -33.296 13.015 43.490 1.00 60.63 A C ANISOU 2377 CD2 LEU A 325 5128 7155 10753 -34 1282 2453 A C ATOM 2378 N ASP A 326 -29.171 15.549 45.727 1.00 63.04 A N ANISOU 2378 N ASP A 326 4865 7685 11401 -394 893 2692 A N ATOM 2379 CA ASP A 326 -28.684 16.740 46.413 1.00 59.36 A C ANISOU 2379 CA ASP A 326 4380 7326 10848 -555 757 2718 A C ATOM 2380 C ASP A 326 -28.192 17.774 45.410 1.00 56.31 A C ANISOU 2380 C ASP A 326 4045 6934 10416 -616 979 2603 A C ATOM 2381 O ASP A 326 -28.362 18.981 45.614 1.00 51.77 A O ANISOU 2381 O ASP A 326 3586 6435 9650 -755 931 2565 A O ATOM 2382 CB ASP A 326 -27.582 16.363 47.403 1.00 59.25 A C ANISOU 2382 CB ASP A 326 4127 7327 11057 -582 561 2868 A C ATOM 2383 CG ASP A 326 -28.079 15.433 48.497 1.00 61.36 A C ANISOU 2383 CG ASP A 326 4377 7600 11335 -559 314 2997 A C ATOM 2384 OD1 ASP A 326 -29.294 15.460 48.792 1.00 59.96 A O ANISOU 2384 OD1 ASP A 326 4381 7471 10931 -582 243 2968 A O ATOM 2385 OD2 ASP A 326 -27.258 14.673 49.056 1.00 61.52 A O1- ANISOU 2385 OD2 ASP A 326 4208 7575 11592 -527 191 3128 A O1- ATOM 2386 N GLN A 327 -27.559 17.315 44.329 1.00 58.23 A N ANISOU 2386 N GLN A 327 4213 7081 10831 -524 1227 2545 A N ATOM 2387 CA GLN A 327 -27.104 18.229 43.287 1.00 61.72 A C ANISOU 2387 CA GLN A 327 4726 7511 11215 -594 1460 2433 A C ATOM 2388 C GLN A 327 -28.280 18.898 42.582 1.00 60.34 A C ANISOU 2388 C GLN A 327 4857 7328 10742 -628 1564 2322 A C ATOM 2389 O GLN A 327 -28.234 20.099 42.292 1.00 60.09 A O ANISOU 2389 O GLN A 327 4952 7330 10549 -760 1613 2266 A O ATOM 2390 CB GLN A 327 -26.230 17.469 42.290 1.00 65.73 A C ANISOU 2390 CB GLN A 327 5098 7912 11964 -488 1714 2385 A C ATOM 2391 CG GLN A 327 -25.821 18.248 41.055 1.00 65.49 A C ANISOU 2391 CG GLN A 327 5170 7855 11859 -558 1994 2257 A C ATOM 2392 CD GLN A 327 -25.091 17.378 40.046 1.00 67.04 A C ANISOU 2392 CD GLN A 327 5257 7937 12276 -446 2262 2191 A C ATOM 2393 NE2 GLN A 327 -25.212 16.064 40.199 1.00 67.73 A N ANISOU 2393 NE2 GLN A 327 5245 7943 12548 -286 2240 2233 A N ATOM 2394 OE1 GLN A 327 -24.430 17.882 39.139 1.00 67.62 A O ANISOU 2394 OE1 GLN A 327 5348 7994 12353 -512 2489 2101 A O ATOM 2395 N LEU A 328 -29.347 18.142 42.307 1.00 58.51 A N ANISOU 2395 N LEU A 328 4754 7042 10434 -517 1591 2295 A N ATOM 2396 CA LEU A 328 -30.525 18.731 41.676 1.00 56.16 A C ANISOU 2396 CA LEU A 328 4751 6728 9860 -542 1666 2199 A C ATOM 2397 C LEU A 328 -31.193 19.755 42.586 1.00 54.57 A C ANISOU 2397 C LEU A 328 4659 6626 9449 -669 1449 2221 A C ATOM 2398 O LEU A 328 -31.621 20.819 42.123 1.00 51.83 A O ANISOU 2398 O LEU A 328 4519 6273 8901 -758 1506 2151 A O ATOM 2399 CB LEU A 328 -31.519 17.638 41.284 1.00 56.97 A C ANISOU 2399 CB LEU A 328 4950 6757 9940 -399 1722 2172 A C ATOM 2400 CG LEU A 328 -31.118 16.727 40.125 1.00 59.41 A C ANISOU 2400 CG LEU A 328 5241 6939 10392 -278 1986 2109 A C ATOM 2401 CD1 LEU A 328 -32.230 15.735 39.833 1.00 59.42 A C ANISOU 2401 CD1 LEU A 328 5366 6873 10337 -156 2016 2084 A C ATOM 2402 CD2 LEU A 328 -30.794 17.547 38.889 1.00 58.77 A C ANISOU 2402 CD2 LEU A 328 5323 6807 10202 -347 2230 1996 A C ATOM 2403 N VAL A 329 -31.293 19.453 43.883 1.00 54.62 A N ANISOU 2403 N VAL A 329 4546 6713 9493 -684 1199 2318 A N ATOM 2404 CA VAL A 329 -31.960 20.365 44.809 1.00 54.14 A C ANISOU 2404 CA VAL A 329 4596 6746 9230 -807 997 2326 A C ATOM 2405 C VAL A 329 -31.202 21.683 44.899 1.00 56.61 A C ANISOU 2405 C VAL A 329 4914 7097 9496 -963 992 2314 A C ATOM 2406 O VAL A 329 -31.802 22.764 44.867 1.00 58.15 A O ANISOU 2406 O VAL A 329 5303 7306 9487 -1061 974 2257 A O ATOM 2407 CB VAL A 329 -32.121 19.705 46.191 1.00 51.81 A C ANISOU 2407 CB VAL A 329 4181 6528 8978 -808 738 2432 A C ATOM 2408 CG1 VAL A 329 -32.695 20.700 47.187 1.00 49.25 A C ANISOU 2408 CG1 VAL A 329 3970 6302 8443 -954 544 2426 A C ATOM 2409 CG2 VAL A 329 -33.012 18.479 46.089 1.00 50.11 A C ANISOU 2409 CG2 VAL A 329 3993 6272 8776 -675 743 2438 A C ATOM 2410 N GLU A 330 -29.874 21.619 45.014 1.00 57.92 A N ANISOU 2410 N GLU A 330 4870 7275 9861 -991 1006 2369 A N ATOM 2411 CA GLU A 330 -29.085 22.838 45.156 1.00 63.03 A C ANISOU 2411 CA GLU A 330 5507 7965 10477 -1152 994 2363 A C ATOM 2412 C GLU A 330 -29.212 23.725 43.923 1.00 61.85 A C ANISOU 2412 C GLU A 330 5557 7749 10193 -1207 1221 2255 A C ATOM 2413 O GLU A 330 -29.433 24.936 44.035 1.00 60.19 A O ANISOU 2413 O GLU A 330 5503 7556 9810 -1344 1182 2223 A O ATOM 2414 CB GLU A 330 -27.620 22.482 45.410 1.00 72.12 A C ANISOU 2414 CB GLU A 330 6377 9133 11891 -1159 985 2441 A C ATOM 2415 CG GLU A 330 -27.380 21.729 46.703 1.00 78.39 A C ANISOU 2415 CG GLU A 330 6993 9981 12812 -1132 729 2573 A C ATOM 2416 CD GLU A 330 -27.547 22.611 47.924 1.00 83.56 A C ANISOU 2416 CD GLU A 330 7707 10733 13309 -1289 483 2617 A C ATOM 2417 OE1 GLU A 330 -27.381 23.843 47.795 1.00 85.59 A O ANISOU 2417 OE1 GLU A 330 8063 11015 13442 -1427 516 2560 A O ATOM 2418 OE2 GLU A 330 -27.847 22.071 49.009 1.00 85.32 A O1- ANISOU 2418 OE2 GLU A 330 7892 11001 13523 -1283 260 2707 A O1- ATOM 2419 N ALA A 331 -29.076 23.136 42.733 1.00 60.16 A N ANISOU 2419 N ALA A 331 5359 7448 10049 -1107 1458 2200 A N ATOM 2420 CA ALA A 331 -29.206 23.915 41.507 1.00 57.66 A C ANISOU 2420 CA ALA A 331 5265 7058 9584 -1168 1674 2103 A C ATOM 2421 C ALA A 331 -30.562 24.605 41.423 1.00 54.82 A C ANISOU 2421 C ALA A 331 5205 6669 8957 -1196 1615 2059 A C ATOM 2422 O ALA A 331 -30.649 25.769 41.014 1.00 55.00 A O ANISOU 2422 O ALA A 331 5421 6658 8817 -1320 1659 2019 A O ATOM 2423 CB ALA A 331 -28.984 23.019 40.289 1.00 57.56 A C ANISOU 2423 CB ALA A 331 5249 6953 9669 -1046 1929 2045 A C ATOM 2424 N ALA A 332 -31.631 23.905 41.812 1.00 54.94 A N ANISOU 2424 N ALA A 332 5261 6687 8926 -1085 1511 2069 A N ATOM 2425 CA ALA A 332 -32.965 24.494 41.749 1.00 56.33 A C ANISOU 2425 CA ALA A 332 5703 6829 8870 -1097 1451 2026 A C ATOM 2426 C ALA A 332 -33.090 25.697 42.676 1.00 61.66 A C ANISOU 2426 C ALA A 332 6431 7566 9431 -1246 1268 2047 A C ATOM 2427 O ALA A 332 -33.756 26.683 42.338 1.00 64.72 A O ANISOU 2427 O ALA A 332 7061 7893 9638 -1309 1273 2006 A O ATOM 2428 CB ALA A 332 -34.021 23.441 42.089 1.00 53.08 A C ANISOU 2428 CB ALA A 332 5289 6427 8453 -959 1369 2035 A C ATOM 2429 N LEU A 333 -32.457 25.637 43.849 1.00 64.29 A N ANISOU 2429 N LEU A 333 6556 8006 9867 -1305 1099 2114 A N ATOM 2430 CA LEU A 333 -32.591 26.719 44.817 1.00 61.90 A C ANISOU 2430 CA LEU A 333 6310 7762 9447 -1450 919 2125 A C ATOM 2431 C LEU A 333 -31.876 27.986 44.366 1.00 62.42 A C ANISOU 2431 C LEU A 333 6467 7788 9464 -1600 1001 2102 A C ATOM 2432 O LEU A 333 -32.173 29.068 44.883 1.00 62.51 A O ANISOU 2432 O LEU A 333 6606 7805 9339 -1722 889 2089 A O ATOM 2433 CB LEU A 333 -32.066 26.269 46.182 1.00 62.35 A C ANISOU 2433 CB LEU A 333 6143 7936 9611 -1480 712 2206 A C ATOM 2434 CG LEU A 333 -32.856 25.130 46.835 1.00 61.22 A C ANISOU 2434 CG LEU A 333 5943 7838 9481 -1369 591 2237 A C ATOM 2435 CD1 LEU A 333 -32.188 24.635 48.114 1.00 62.93 A C ANISOU 2435 CD1 LEU A 333 5955 8150 9806 -1406 388 2337 A C ATOM 2436 CD2 LEU A 333 -34.281 25.567 47.104 1.00 55.99 A C ANISOU 2436 CD2 LEU A 333 5489 7179 8607 -1385 515 2177 A C ATOM 2437 N ALA A 334 -30.940 27.877 43.423 1.00 60.43 A N ANISOU 2437 N ALA A 334 6156 7491 9313 -1603 1197 2090 A N ATOM 2438 CA ALA A 334 -30.270 29.053 42.885 1.00 58.04 A C ANISOU 2438 CA ALA A 334 5959 7145 8949 -1760 1298 2063 A C ATOM 2439 C ALA A 334 -31.139 29.813 41.891 1.00 56.60 A C ANISOU 2439 C ALA A 334 6114 6835 8558 -1781 1402 2003 A C ATOM 2440 O ALA A 334 -30.877 30.994 41.636 1.00 61.31 A O ANISOU 2440 O ALA A 334 6867 7379 9049 -1930 1428 1987 A O ATOM 2441 CB ALA A 334 -28.950 28.654 42.222 1.00 54.17 A C ANISOU 2441 CB ALA A 334 5284 6661 8637 -1770 1479 2067 A C ATOM 2442 N VAL A 335 -32.161 29.173 41.339 1.00 53.77 A N ANISOU 2442 N VAL A 335 5882 6413 8135 -1638 1449 1974 A N ATOM 2443 CA VAL A 335 -32.994 29.803 40.312 1.00 51.81 A C ANISOU 2443 CA VAL A 335 5971 6022 7694 -1637 1539 1923 A C ATOM 2444 C VAL A 335 -33.948 30.789 40.983 1.00 51.17 A C ANISOU 2444 C VAL A 335 6068 5912 7464 -1691 1349 1930 A C ATOM 2445 O VAL A 335 -34.642 30.412 41.941 1.00 53.60 A O ANISOU 2445 O VAL A 335 6303 6301 7763 -1619 1169 1917 A O ATOM 2446 CB VAL A 335 -33.764 28.745 39.527 1.00 50.23 A C ANISOU 2446 CB VAL A 335 5847 5757 7479 -1458 1642 1884 A C ATOM 2447 CG1 VAL A 335 -34.658 29.400 38.489 1.00 50.61 A C ANISOU 2447 CG1 VAL A 335 6274 5642 7313 -1448 1707 1824 A C ATOM 2448 CG2 VAL A 335 -32.806 27.759 38.868 1.00 50.09 A C ANISOU 2448 CG2 VAL A 335 5652 5762 7619 -1402 1829 1870 A C ATOM 2449 N PRO A 336 -34.015 32.034 40.519 1.00 48.62 A N ANISOU 2449 N PRO A 336 6010 5487 6978 -1794 1349 1883 A N ATOM 2450 CA PRO A 336 -35.020 32.964 41.045 1.00 47.61 A C ANISOU 2450 CA PRO A 336 6103 5321 6664 -1789 1136 1801 A C ATOM 2451 C PRO A 336 -36.424 32.539 40.648 1.00 46.39 A C ANISOU 2451 C PRO A 336 6138 5104 6385 -1594 1075 1696 A C ATOM 2452 O PRO A 336 -36.654 31.991 39.568 1.00 46.49 A O ANISOU 2452 O PRO A 336 6259 5036 6370 -1502 1209 1671 A O ATOM 2453 CB PRO A 336 -34.639 34.305 40.404 1.00 43.00 A C ANISOU 2453 CB PRO A 336 5769 4611 5957 -1941 1183 1787 A C ATOM 2454 CG PRO A 336 -33.210 34.138 39.971 1.00 51.74 A C ANISOU 2454 CG PRO A 336 6695 5748 7218 -2078 1394 1884 A C ATOM 2455 CD PRO A 336 -33.069 32.693 39.605 1.00 52.56 A C ANISOU 2455 CD PRO A 336 6598 5907 7466 -1938 1532 1902 A C ATOM 2456 N GLY A 337 -37.373 32.799 41.546 1.00 44.70 A N ANISOU 2456 N GLY A 337 5961 4927 6097 -1541 873 1627 A N ATOM 2457 CA GLY A 337 -38.731 32.337 41.373 1.00 37.45 A C ANISOU 2457 CA GLY A 337 5161 3976 5092 -1360 794 1525 A C ATOM 2458 C GLY A 337 -39.005 30.974 41.966 1.00 44.13 A C ANISOU 2458 C GLY A 337 5768 4951 6047 -1255 778 1549 A C ATOM 2459 O GLY A 337 -40.175 30.582 42.065 1.00 45.15 A O ANISOU 2459 O GLY A 337 5961 5081 6112 -1121 691 1461 A O ATOM 2460 N VAL A 338 -37.968 30.239 42.359 1.00 43.99 A N ANISOU 2460 N VAL A 338 5476 5037 6203 -1313 854 1665 A N ATOM 2461 CA VAL A 338 -38.138 28.939 42.997 1.00 43.84 A C ANISOU 2461 CA VAL A 338 5228 5131 6298 -1227 823 1706 A C ATOM 2462 C VAL A 338 -38.390 29.144 44.485 1.00 44.21 A C ANISOU 2462 C VAL A 338 5165 5302 6332 -1297 627 1710 A C ATOM 2463 O VAL A 338 -37.619 29.825 45.170 1.00 49.73 A O ANISOU 2463 O VAL A 338 5783 6050 7061 -1454 570 1770 A O ATOM 2464 CB VAL A 338 -36.906 28.052 42.761 1.00 37.29 A C ANISOU 2464 CB VAL A 338 4148 4340 5682 -1250 977 1832 A C ATOM 2465 CG1 VAL A 338 -36.981 26.800 43.622 1.00 36.93 A C ANISOU 2465 CG1 VAL A 338 3856 4407 5766 -1184 902 1895 A C ATOM 2466 CG2 VAL A 338 -36.780 27.692 41.287 1.00 41.27 A C ANISOU 2466 CG2 VAL A 338 4774 4723 6185 -1174 1194 1805 A C ATOM 2467 N TYR A 339 -39.476 28.550 44.988 1.00 45.57 A N ANISOU 2467 N TYR A 339 5340 5524 6450 -1196 529 1643 A N ATOM 2468 CA TYR A 339 -39.783 28.643 46.412 1.00 45.23 A C ANISOU 2468 CA TYR A 339 5207 5603 6376 -1273 361 1636 A C ATOM 2469 C TYR A 339 -39.037 27.593 47.226 1.00 47.11 A C ANISOU 2469 C TYR A 339 5166 5965 6771 -1324 329 1778 A C ATOM 2470 O TYR A 339 -38.586 27.876 48.341 1.00 49.24 A O ANISOU 2470 O TYR A 339 5328 6328 7051 -1469 209 1838 A O ATOM 2471 CB TYR A 339 -41.289 28.505 46.639 1.00 43.60 A C ANISOU 2471 CB TYR A 339 5123 5401 6043 -1161 278 1491 A C ATOM 2472 CG TYR A 339 -42.117 29.579 45.974 1.00 45.61 A C ANISOU 2472 CG TYR A 339 5641 5528 6160 -1103 264 1347 A C ATOM 2473 CD1 TYR A 339 -42.171 30.862 46.504 1.00 46.44 A C ANISOU 2473 CD1 TYR A 339 5855 5611 6179 -1204 177 1283 A C ATOM 2474 CD2 TYR A 339 -42.853 29.311 44.827 1.00 42.24 A C ANISOU 2474 CD2 TYR A 339 5363 4994 5694 -950 324 1278 A C ATOM 2475 CE1 TYR A 339 -42.930 31.853 45.906 1.00 44.89 A C ANISOU 2475 CE1 TYR A 339 5900 5278 5876 -1141 147 1154 A C ATOM 2476 CE2 TYR A 339 -43.614 30.295 44.221 1.00 41.06 A C ANISOU 2476 CE2 TYR A 339 5456 4714 5430 -894 281 1158 A C ATOM 2477 CZ TYR A 339 -43.648 31.561 44.765 1.00 43.03 A C ANISOU 2477 CZ TYR A 339 5802 4935 5612 -983 191 1098 A C ATOM 2478 OH TYR A 339 -44.407 32.533 44.158 1.00 45.39 A O ANISOU 2478 OH TYR A 339 6342 5086 5817 -916 133 982 A O ATOM 2479 N GLY A 340 -38.894 26.388 46.690 1.00 44.94 A N ANISOU 2479 N GLY A 340 4781 5680 6616 -1212 424 1835 A N ATOM 2480 CA GLY A 340 -38.203 25.329 47.404 1.00 45.83 A C ANISOU 2480 CA GLY A 340 4630 5886 6898 -1241 382 1977 A C ATOM 2481 C GLY A 340 -38.112 24.099 46.530 1.00 45.01 A C ANISOU 2481 C GLY A 340 4452 5725 6923 -1090 523 2010 A C ATOM 2482 O GLY A 340 -38.734 24.013 45.466 1.00 46.84 A O ANISOU 2482 O GLY A 340 4851 5861 7083 -970 637 1915 A O ATOM 2483 N SER A 341 -37.313 23.141 46.996 1.00 35.75 A N ANISOU 2483 N SER A 341 3049 4604 5929 -1083 494 2122 A N ATOM 2484 CA SER A 341 -37.107 21.904 46.257 1.00 35.95 A C ANISOU 2484 CA SER A 341 2991 4570 6097 -934 620 2145 A C ATOM 2485 C SER A 341 -36.589 20.843 47.215 1.00 48.20 A C ANISOU 2485 C SER A 341 4336 6190 7787 -915 484 2238 A C ATOM 2486 O SER A 341 -35.952 21.153 48.225 1.00 52.88 A O ANISOU 2486 O SER A 341 4831 6860 8400 -1019 329 2298 A O ATOM 2487 CB SER A 341 -36.131 22.096 45.089 1.00 42.42 A C ANISOU 2487 CB SER A 341 3799 5297 7021 -902 825 2134 A C ATOM 2488 OG SER A 341 -36.052 20.927 44.289 1.00 43.52 A O ANISOU 2488 OG SER A 341 3889 5363 7282 -758 971 2133 A O ATOM 2489 N ARG A 342 -36.876 19.588 46.884 1.00 51.48 A N ANISOU 2489 N ARG A 342 4703 6564 8292 -785 538 2258 A N ATOM 2490 CA ARG A 342 -36.484 18.460 47.718 1.00 48.24 A C ANISOU 2490 CA ARG A 342 4119 6190 8020 -755 407 2364 A C ATOM 2491 C ARG A 342 -36.750 17.180 46.944 1.00 52.07 A C ANISOU 2491 C ARG A 342 4580 6585 8620 -598 537 2368 A C ATOM 2492 O ARG A 342 -37.484 17.176 45.951 1.00 54.18 A O ANISOU 2492 O ARG A 342 4992 6785 8810 -528 695 2280 A O ATOM 2493 CB ARG A 342 -37.246 18.443 49.045 1.00 44.20 A C ANISOU 2493 CB ARG A 342 3644 5787 7362 -853 185 2383 A C ATOM 2494 CG ARG A 342 -38.751 18.313 48.878 1.00 45.13 A C ANISOU 2494 CG ARG A 342 3924 5913 7310 -828 209 2293 A C ATOM 2495 CD ARG A 342 -39.443 18.083 50.212 1.00 46.47 A C ANISOU 2495 CD ARG A 342 4111 6193 7352 -928 9 2309 A C ATOM 2496 NE ARG A 342 -40.601 17.207 50.071 1.00 47.53 A N ANISOU 2496 NE ARG A 342 4309 6322 7427 -864 32 2271 A N ATOM 2497 CZ ARG A 342 -40.585 15.902 50.324 1.00 52.79 A C ANISOU 2497 CZ ARG A 342 4894 6973 8190 -808 -15 2352 A C ATOM 2498 NH1 ARG A 342 -39.473 15.318 50.751 1.00 58.00 A N1+ ANISOU 2498 NH1 ARG A 342 5399 7617 9021 -802 -96 2485 A N1+ ATOM 2499 NH2 ARG A 342 -41.683 15.181 50.163 1.00 53.59 A N ANISOU 2499 NH2 ARG A 342 5075 7068 8217 -758 11 2300 A N ATOM 2500 N MET A 343 -36.145 16.095 47.413 1.00 54.55 A N ANISOU 2500 N MET A 343 4720 6885 9120 -547 462 2477 A N ATOM 2501 CA MET A 343 -36.439 14.782 46.863 1.00 55.52 A C ANISOU 2501 CA MET A 343 4815 6919 9360 -407 558 2493 A C ATOM 2502 C MET A 343 -37.844 14.341 47.252 1.00 52.39 A C ANISOU 2502 C MET A 343 4545 6565 8795 -415 475 2463 A C ATOM 2503 O MET A 343 -38.390 14.754 48.279 1.00 52.12 A O ANISOU 2503 O MET A 343 4560 6639 8604 -531 296 2468 A O ATOM 2504 CB MET A 343 -35.428 13.751 47.358 1.00 60.17 A C ANISOU 2504 CB MET A 343 5184 7468 10210 -357 476 2635 A C ATOM 2505 CG MET A 343 -35.346 13.656 48.871 1.00 64.87 A C ANISOU 2505 CG MET A 343 5714 8160 10774 -470 191 2755 A C ATOM 2506 SD MET A 343 -34.787 12.036 49.441 1.00 68.50 A S ANISOU 2506 SD MET A 343 5989 8540 11499 -394 68 2934 A S ATOM 2507 CE MET A 343 -36.303 11.083 49.330 1.00 65.22 A C ANISOU 2507 CE MET A 343 5708 8114 10958 -346 83 2894 A C ATOM 2508 N THR A 344 -38.431 13.497 46.411 1.00 52.64 A N ANISOU 2508 N THR A 344 4637 6508 8855 -299 619 2424 A N ATOM 2509 CA THR A 344 -39.714 12.878 46.696 1.00 50.28 A C ANISOU 2509 CA THR A 344 4451 6234 8418 -292 551 2392 A C ATOM 2510 C THR A 344 -39.590 11.376 46.494 1.00 50.90 A C ANISOU 2510 C THR A 344 4448 6219 8673 -178 587 2458 A C ATOM 2511 O THR A 344 -38.655 10.888 45.854 1.00 56.34 A O ANISOU 2511 O THR A 344 5008 6805 9594 -87 727 2507 A O ATOM 2512 CB THR A 344 -40.837 13.442 45.814 1.00 48.74 A C ANISOU 2512 CB THR A 344 4514 6015 7989 -245 652 2206 A C ATOM 2513 CG2 THR A 344 -41.196 14.847 46.254 1.00 49.50 A C ANISOU 2513 CG2 THR A 344 4706 6206 7898 -360 566 2137 A C ATOM 2514 OG1 THR A 344 -40.409 13.467 44.447 1.00 50.61 A O ANISOU 2514 OG1 THR A 344 4805 6129 8294 -145 878 2150 A O ATOM 2515 N GLY A 345 -40.554 10.648 47.039 1.00 49.01 A N ANISOU 2515 N GLY A 345 4287 6011 8325 -187 470 2450 A N ATOM 2516 CA GLY A 345 -40.518 9.205 46.961 1.00 54.25 A C ANISOU 2516 CA GLY A 345 4893 6580 9139 -93 477 2518 A C ATOM 2517 C GLY A 345 -39.600 8.607 48.012 1.00 58.56 A C ANISOU 2517 C GLY A 345 5214 7139 9899 -144 305 2718 A C ATOM 2518 O GLY A 345 -39.236 9.244 49.007 1.00 61.49 A O ANISOU 2518 O GLY A 345 5502 7617 10244 -282 138 2803 A O ATOM 2519 N GLY A 346 -39.213 7.354 47.772 1.00 59.38 A N ANISOU 2519 N GLY A 346 5225 7116 10219 -31 339 2795 A N ATOM 2520 CA GLY A 346 -38.403 6.643 48.749 1.00 58.89 A C ANISOU 2520 CA GLY A 346 4956 7039 10378 -64 148 2996 A C ATOM 2521 C GLY A 346 -37.003 7.208 48.903 1.00 59.81 A C ANISOU 2521 C GLY A 346 4889 7148 10686 -72 127 3075 A C ATOM 2522 O GLY A 346 -36.462 7.249 50.012 1.00 59.70 A O ANISOU 2522 O GLY A 346 4799 7181 10701 -172 -102 3206 A O ATOM 2523 N GLY A 347 -36.400 7.651 47.810 1.00 61.80 A N ANISOU 2523 N GLY A 347 5122 7331 11027 24 357 2979 A N ATOM 2524 CA GLY A 347 -35.049 8.176 47.839 1.00 65.87 A C ANISOU 2524 CA GLY A 347 5502 7825 11701 20 360 3018 A C ATOM 2525 C GLY A 347 -34.071 7.237 47.155 1.00 68.98 A C ANISOU 2525 C GLY A 347 5751 8045 12414 168 507 3044 A C ATOM 2526 O GLY A 347 -34.446 6.279 46.474 1.00 70.49 A O ANISOU 2526 O GLY A 347 5971 8122 12688 287 648 3005 A O ATOM 2527 N PHE A 348 -32.784 7.534 47.348 1.00 70.81 A N ANISOU 2527 N PHE A 348 5826 8252 12824 153 478 3101 A N ATOM 2528 CA PHE A 348 -31.708 6.750 46.745 1.00 73.28 A C ANISOU 2528 CA PHE A 348 5984 8404 13455 276 620 3110 A C ATOM 2529 C PHE A 348 -31.742 6.852 45.225 1.00 74.92 A C ANISOU 2529 C PHE A 348 6267 8529 13670 386 966 2935 A C ATOM 2530 O PHE A 348 -31.340 5.925 44.516 1.00 78.73 A O ANISOU 2530 O PHE A 348 6695 8860 14358 509 1136 2898 A O ATOM 2531 CB PHE A 348 -31.771 5.285 47.187 1.00 74.17 A C ANISOU 2531 CB PHE A 348 6035 8404 13742 337 510 3217 A C ATOM 2532 N GLY A 349 -32.223 7.987 44.723 1.00 69.89 A N ANISOU 2532 N GLY A 349 5774 7986 12795 328 1071 2819 A N ATOM 2533 CA GLY A 349 -32.507 8.212 43.327 1.00 67.30 A C ANISOU 2533 CA GLY A 349 5587 7596 12388 393 1377 2651 A C ATOM 2534 C GLY A 349 -33.911 8.749 43.172 1.00 64.56 A C ANISOU 2534 C GLY A 349 5470 7336 11722 341 1376 2573 A C ATOM 2535 O GLY A 349 -34.529 9.217 44.136 1.00 63.61 A O ANISOU 2535 O GLY A 349 5389 7346 11435 236 1152 2629 A O ATOM 2536 N GLY A 350 -34.425 8.675 41.949 1.00 63.16 A N ANISOU 2536 N GLY A 350 5462 7082 11454 406 1629 2436 A N ATOM 2537 CA GLY A 350 -35.773 9.133 41.675 1.00 61.35 A C ANISOU 2537 CA GLY A 350 5469 6911 10929 361 1643 2354 A C ATOM 2538 C GLY A 350 -35.879 10.573 41.214 1.00 58.16 A C ANISOU 2538 C GLY A 350 5218 6574 10305 263 1706 2259 A C ATOM 2539 O GLY A 350 -35.049 11.042 40.430 1.00 58.87 A O ANISOU 2539 O GLY A 350 5306 6613 10448 264 1884 2195 A O ATOM 2540 N CYS A 351 -36.896 11.285 41.694 1.00 56.22 A N ANISOU 2540 N CYS A 351 5113 6435 9813 171 1561 2245 A N ATOM 2541 CA CYS A 351 -37.249 12.600 41.178 1.00 54.90 A C ANISOU 2541 CA CYS A 351 5140 6304 9417 88 1618 2148 A C ATOM 2542 C CYS A 351 -37.098 13.670 42.256 1.00 50.53 A C ANISOU 2542 C CYS A 351 4528 5889 8783 -44 1400 2198 A C ATOM 2543 O CYS A 351 -36.966 13.379 43.448 1.00 48.03 A O ANISOU 2543 O CYS A 351 4064 5653 8532 -83 1188 2300 A O ATOM 2544 CB CYS A 351 -38.683 12.605 40.630 1.00 53.72 A C ANISOU 2544 CB CYS A 351 5285 6130 8998 117 1622 2027 A C ATOM 2545 SG CYS A 351 -38.920 11.686 39.089 1.00 58.73 A S ANISOU 2545 SG CYS A 351 6098 6590 9626 245 1889 1914 A S ATOM 2546 N THR A 352 -37.108 14.924 41.806 1.00 48.35 A N ANISOU 2546 N THR A 352 4390 5628 8353 -122 1458 2126 A N ATOM 2547 CA THR A 352 -37.124 16.096 42.671 1.00 47.83 A C ANISOU 2547 CA THR A 352 4326 5676 8171 -256 1282 2147 A C ATOM 2548 C THR A 352 -38.360 16.928 42.350 1.00 47.65 A C ANISOU 2548 C THR A 352 4569 5657 7879 -290 1267 2048 A C ATOM 2549 O THR A 352 -38.663 17.167 41.176 1.00 51.47 A O ANISOU 2549 O THR A 352 5255 6044 8255 -243 1424 1946 A O ATOM 2550 CB THR A 352 -35.851 16.935 42.497 1.00 49.07 A C ANISOU 2550 CB THR A 352 4395 5838 8411 -327 1342 2153 A C ATOM 2551 CG2 THR A 352 -36.027 17.954 41.386 1.00 47.90 A C ANISOU 2551 CG2 THR A 352 4469 5628 8103 -368 1513 2051 A C ATOM 2552 OG1 THR A 352 -35.560 17.627 43.717 1.00 52.27 A O ANISOU 2552 OG1 THR A 352 4705 6361 8793 -447 1123 2218 A O ATOM 2553 N VAL A 353 -39.087 17.338 43.387 1.00 43.04 A N ANISOU 2553 N VAL A 353 4016 5177 7159 -357 1052 2042 A N ATOM 2554 CA VAL A 353 -40.242 18.217 43.243 1.00 43.26 A C ANISOU 2554 CA VAL A 353 4291 5215 6930 -371 985 1910 A C ATOM 2555 C VAL A 353 -39.822 19.635 43.604 1.00 46.69 A C ANISOU 2555 C VAL A 353 4747 5693 7299 -500 928 1912 A C ATOM 2556 O VAL A 353 -39.150 19.852 44.621 1.00 45.51 A O ANISOU 2556 O VAL A 353 4423 5632 7236 -606 819 2011 A O ATOM 2557 CB VAL A 353 -41.413 17.755 44.126 1.00 40.24 A C ANISOU 2557 CB VAL A 353 3936 4914 6438 -362 809 1875 A C ATOM 2558 CG1 VAL A 353 -41.031 17.838 45.591 1.00 38.07 A C ANISOU 2558 CG1 VAL A 353 3485 4765 6214 -483 633 1978 A C ATOM 2559 CG2 VAL A 353 -42.645 18.596 43.849 1.00 40.28 A C ANISOU 2559 CG2 VAL A 353 4177 4913 6213 -350 757 1721 A C ATOM 2560 N THR A 354 -40.223 20.601 42.780 1.00 47.47 A N ANISOU 2560 N THR A 354 5073 5722 7243 -500 987 1806 A N ATOM 2561 CA THR A 354 -39.844 21.997 42.960 1.00 43.13 A C ANISOU 2561 CA THR A 354 4582 5183 6621 -619 949 1797 A C ATOM 2562 C THR A 354 -41.079 22.867 42.786 1.00 42.59 A C ANISOU 2562 C THR A 354 4769 5084 6328 -599 858 1657 A C ATOM 2563 O THR A 354 -41.741 22.808 41.745 1.00 42.74 A O ANISOU 2563 O THR A 354 4984 5004 6253 -508 928 1570 A O ATOM 2564 CB THR A 354 -38.755 22.412 41.966 1.00 47.71 A C ANISOU 2564 CB THR A 354 5174 5676 7278 -657 1144 1829 A C ATOM 2565 CG2 THR A 354 -38.428 23.887 42.125 1.00 48.32 A C ANISOU 2565 CG2 THR A 354 5341 5754 7264 -791 1098 1816 A C ATOM 2566 OG1 THR A 354 -37.573 21.634 42.193 1.00 53.03 A O ANISOU 2566 OG1 THR A 354 5571 6380 8198 -671 1224 1953 A O ATOM 2567 N LEU A 355 -41.387 23.670 43.800 1.00 41.97 A N ANISOU 2567 N LEU A 355 4691 5085 6172 -686 700 1632 A N ATOM 2568 CA LEU A 355 -42.464 24.649 43.738 1.00 37.86 A C ANISOU 2568 CA LEU A 355 4387 4528 5469 -671 608 1494 A C ATOM 2569 C LEU A 355 -41.876 25.999 43.342 1.00 41.19 A C ANISOU 2569 C LEU A 355 4933 4876 5840 -762 636 1488 A C ATOM 2570 O LEU A 355 -40.950 26.489 43.997 1.00 46.98 A O ANISOU 2570 O LEU A 355 5550 5666 6635 -893 614 1567 A O ATOM 2571 CB LEU A 355 -43.175 24.753 45.090 1.00 36.50 A C ANISOU 2571 CB LEU A 355 4152 4477 5241 -718 438 1449 A C ATOM 2572 CG LEU A 355 -44.628 25.235 45.110 1.00 37.75 A C ANISOU 2572 CG LEU A 355 4479 4615 5252 -648 346 1282 A C ATOM 2573 CD1 LEU A 355 -45.537 24.168 44.511 1.00 37.61 A C ANISOU 2573 CD1 LEU A 355 4493 4572 5227 -507 376 1231 A C ATOM 2574 CD2 LEU A 355 -45.080 25.600 46.519 1.00 38.69 A C ANISOU 2574 CD2 LEU A 355 4533 4853 5315 -740 211 1232 A C ATOM 2575 N LEU A 356 -42.408 26.597 42.276 1.00 41.79 A N ANISOU 2575 N LEU A 356 5255 4822 5802 -703 673 1399 A N ATOM 2576 CA LEU A 356 -41.808 27.801 41.713 1.00 41.71 A C ANISOU 2576 CA LEU A 356 5395 4716 5739 -793 719 1404 A C ATOM 2577 C LEU A 356 -42.868 28.644 41.022 1.00 42.96 A C ANISOU 2577 C LEU A 356 5844 4746 5734 -725 645 1279 A C ATOM 2578 O LEU A 356 -43.973 28.178 40.733 1.00 43.40 A O ANISOU 2578 O LEU A 356 5978 4776 5736 -598 591 1195 A O ATOM 2579 CB LEU A 356 -40.675 27.473 40.729 1.00 43.16 A C ANISOU 2579 CB LEU A 356 5554 4838 6007 -827 926 1492 A C ATOM 2580 CG LEU A 356 -40.919 26.549 39.526 1.00 46.05 A C ANISOU 2580 CG LEU A 356 6011 5117 6367 -714 1070 1473 A C ATOM 2581 CD1 LEU A 356 -42.024 27.048 38.601 1.00 50.21 A C ANISOU 2581 CD1 LEU A 356 6856 5513 6710 -639 1018 1361 A C ATOM 2582 CD2 LEU A 356 -39.620 26.361 38.745 1.00 50.16 A C ANISOU 2582 CD2 LEU A 356 6476 5592 6989 -784 1297 1553 A C ATOM 2583 N GLU A 357 -42.512 29.903 40.768 1.00 45.34 A N ANISOU 2583 N GLU A 357 6303 4960 5966 -817 631 1271 A N ATOM 2584 CA GLU A 357 -43.350 30.781 39.964 1.00 45.31 A C ANISOU 2584 CA GLU A 357 6596 4798 5819 -761 559 1173 A C ATOM 2585 C GLU A 357 -43.452 30.242 38.543 1.00 43.65 A C ANISOU 2585 C GLU A 357 6550 4475 5562 -692 676 1180 A C ATOM 2586 O GLU A 357 -42.445 29.852 37.945 1.00 40.02 A O ANISOU 2586 O GLU A 357 6054 4003 5150 -757 858 1266 A O ATOM 2587 CB GLU A 357 -42.769 32.194 39.939 1.00 51.22 A C ANISOU 2587 CB GLU A 357 7488 5463 6510 -894 535 1185 A C ATOM 2588 CG GLU A 357 -42.476 32.792 41.298 1.00 54.63 A C ANISOU 2588 CG GLU A 357 7777 5999 6980 -998 438 1186 A C ATOM 2589 CD GLU A 357 -41.768 34.128 41.186 1.00 59.18 A C ANISOU 2589 CD GLU A 357 8498 6484 7504 -1147 434 1210 A C ATOM 2590 OE1 GLU A 357 -41.346 34.480 40.062 1.00 61.61 A O ANISOU 2590 OE1 GLU A 357 8987 6663 7758 -1185 530 1245 A O ATOM 2591 OE2 GLU A 357 -41.636 34.825 42.214 1.00 60.28 A O1- ANISOU 2591 OE2 GLU A 357 8584 6676 7644 -1238 338 1190 A O1- ATOM 2592 N ALA A 358 -44.674 30.205 38.005 1.00 43.77 A N ANISOU 2592 N ALA A 358 6741 4404 5484 -566 573 1085 A N ATOM 2593 CA ALA A 358 -44.873 29.653 36.668 1.00 41.68 A C ANISOU 2593 CA ALA A 358 6656 4029 5153 -508 664 1086 A C ATOM 2594 C ALA A 358 -43.920 30.292 35.666 1.00 43.22 A C ANISOU 2594 C ALA A 358 7045 4100 5278 -631 802 1149 A C ATOM 2595 O ALA A 358 -43.361 29.609 34.801 1.00 44.29 A O ANISOU 2595 O ALA A 358 7213 4201 5412 -654 989 1195 A O ATOM 2596 CB ALA A 358 -46.325 29.838 36.226 1.00 44.70 A C ANISOU 2596 CB ALA A 358 7233 4315 5436 -377 487 977 A C ATOM 2597 N SER A 359 -43.731 31.610 35.765 1.00 45.66 A N ANISOU 2597 N SER A 359 7494 4331 5522 -720 723 1145 A N ATOM 2598 CA SER A 359 -42.848 32.318 34.846 1.00 46.14 A C ANISOU 2598 CA SER A 359 7761 4270 5500 -862 849 1203 A C ATOM 2599 C SER A 359 -41.408 31.824 34.928 1.00 50.72 A C ANISOU 2599 C SER A 359 8127 4946 6199 -984 1088 1302 A C ATOM 2600 O SER A 359 -40.661 31.967 33.954 1.00 54.99 A O ANISOU 2600 O SER A 359 8808 5400 6685 -1090 1265 1345 A O ATOM 2601 CB SER A 359 -42.897 33.822 35.130 1.00 46.30 A C ANISOU 2601 CB SER A 359 7945 4199 5448 -941 703 1183 A C ATOM 2602 OG SER A 359 -42.633 34.099 36.496 1.00 47.75 A O ANISOU 2602 OG SER A 359 7887 4517 5738 -978 637 1183 A O ATOM 2603 N ALA A 360 -40.998 31.260 36.065 1.00 50.23 A N ANISOU 2603 N ALA A 360 7729 5056 6302 -980 1094 1338 A N ATOM 2604 CA ALA A 360 -39.621 30.819 36.249 1.00 49.68 A C ANISOU 2604 CA ALA A 360 7415 5077 6383 -1088 1289 1436 A C ATOM 2605 C ALA A 360 -39.348 29.420 35.705 1.00 50.92 A C ANISOU 2605 C ALA A 360 7447 5265 6637 -1013 1476 1460 A C ATOM 2606 O ALA A 360 -38.181 29.016 35.653 1.00 52.53 A O ANISOU 2606 O ALA A 360 7459 5518 6982 -1090 1666 1532 A O ATOM 2607 CB ALA A 360 -39.249 30.869 37.734 1.00 47.31 A C ANISOU 2607 CB ALA A 360 6819 4936 6219 -1130 1186 1478 A C ATOM 2608 N ALA A 361 -40.379 28.678 35.297 1.00 49.60 A N ANISOU 2608 N ALA A 361 7376 5063 6407 -868 1430 1397 A N ATOM 2609 CA ALA A 361 -40.174 27.290 34.883 1.00 48.33 A C ANISOU 2609 CA ALA A 361 7091 4928 6343 -791 1596 1412 A C ATOM 2610 C ALA A 361 -39.174 27.148 33.745 1.00 48.93 A C ANISOU 2610 C ALA A 361 7247 4920 6423 -882 1874 1441 A C ATOM 2611 O ALA A 361 -38.234 26.344 33.873 1.00 48.49 A O ANISOU 2611 O ALA A 361 6938 4931 6555 -893 2054 1495 A O ATOM 2612 CB ALA A 361 -41.520 26.663 34.510 1.00 47.71 A C ANISOU 2612 CB ALA A 361 7159 4805 6164 -641 1488 1331 A C ATOM 2613 N PRO A 362 -39.304 27.866 32.628 1.00 47.58 A N ANISOU 2613 N PRO A 362 7416 4600 6061 -953 1927 1407 A N ATOM 2614 CA PRO A 362 -38.328 27.697 31.538 1.00 49.11 A C ANISOU 2614 CA PRO A 362 7655 4759 6247 -1037 2164 1391 A C ATOM 2615 C PRO A 362 -36.888 27.896 31.982 1.00 49.97 A C ANISOU 2615 C PRO A 362 7478 4975 6533 -1149 2286 1445 A C ATOM 2616 O PRO A 362 -36.015 27.100 31.616 1.00 51.99 A O ANISOU 2616 O PRO A 362 7556 5276 6921 -1144 2481 1435 A O ATOM 2617 CB PRO A 362 -38.769 28.753 30.515 1.00 49.15 A C ANISOU 2617 CB PRO A 362 8055 4623 5998 -1106 2089 1337 A C ATOM 2618 CG PRO A 362 -40.231 28.935 30.777 1.00 48.22 A C ANISOU 2618 CG PRO A 362 8128 4431 5763 -999 1849 1313 A C ATOM 2619 CD PRO A 362 -40.396 28.784 32.264 1.00 49.13 A C ANISOU 2619 CD PRO A 362 7944 4680 6042 -933 1717 1348 A C ATOM 2620 N HIS A 363 -36.614 28.945 32.761 1.00 49.81 A N ANISOU 2620 N HIS A 363 7412 4989 6525 -1250 2170 1497 A N ATOM 2621 CA HIS A 363 -35.254 29.170 33.240 1.00 52.50 A C ANISOU 2621 CA HIS A 363 7473 5439 7035 -1366 2254 1553 A C ATOM 2622 C HIS A 363 -34.815 28.075 34.205 1.00 53.09 A C ANISOU 2622 C HIS A 363 7153 5653 7367 -1287 2269 1605 A C ATOM 2623 O HIS A 363 -33.671 27.608 34.144 1.00 53.00 A O ANISOU 2623 O HIS A 363 6900 5715 7524 -1317 2408 1617 A O ATOM 2624 CB HIS A 363 -35.150 30.537 33.914 1.00 54.84 A C ANISOU 2624 CB HIS A 363 7827 5733 7275 -1497 2104 1595 A C ATOM 2625 CG HIS A 363 -33.800 30.819 34.497 1.00 61.70 A C ANISOU 2625 CG HIS A 363 8410 6722 8313 -1630 2157 1659 A C ATOM 2626 CD2 HIS A 363 -32.557 30.523 34.048 1.00 64.86 A C ANISOU 2626 CD2 HIS A 363 8632 7182 8831 -1697 2339 1663 A C ATOM 2627 ND1 HIS A 363 -33.627 31.484 35.692 1.00 62.81 A N ANISOU 2627 ND1 HIS A 363 8419 6930 8515 -1714 2005 1723 A N ATOM 2628 CE1 HIS A 363 -32.337 31.588 35.953 1.00 64.58 A C ANISOU 2628 CE1 HIS A 363 8398 7257 8881 -1832 2074 1768 A C ATOM 2629 NE2 HIS A 363 -31.665 31.012 34.972 1.00 65.59 A N ANISOU 2629 NE2 HIS A 363 8487 7383 9053 -1818 2278 1732 A N ATOM 2630 N ALA A 364 -35.711 27.647 35.098 1.00 50.39 A N ANISOU 2630 N ALA A 364 6740 5345 7060 -1181 2117 1633 A N ATOM 2631 CA ALA A 364 -35.347 26.624 36.073 1.00 50.02 A C ANISOU 2631 CA ALA A 364 6328 5431 7246 -1106 2085 1689 A C ATOM 2632 C ALA A 364 -34.895 25.341 35.386 1.00 53.74 A C ANISOU 2632 C ALA A 364 6682 5898 7838 -1007 2270 1655 A C ATOM 2633 O ALA A 364 -33.892 24.737 35.784 1.00 58.37 A O ANISOU 2633 O ALA A 364 6966 6569 8641 -999 2323 1690 A O ATOM 2634 CB ALA A 364 -36.522 26.351 37.012 1.00 45.47 A C ANISOU 2634 CB ALA A 364 5737 4899 6642 -1003 1868 1697 A C ATOM 2635 N MET A 365 -35.621 24.910 34.352 1.00 54.02 A N ANISOU 2635 N MET A 365 6963 5824 7739 -929 2362 1582 A N ATOM 2636 CA MET A 365 -35.230 23.700 33.634 1.00 53.14 A C ANISOU 2636 CA MET A 365 6773 5687 7733 -839 2555 1537 A C ATOM 2637 C MET A 365 -33.870 23.871 32.971 1.00 52.91 A C ANISOU 2637 C MET A 365 6661 5657 7786 -932 2760 1511 A C ATOM 2638 O MET A 365 -33.048 22.947 32.975 1.00 53.25 A O ANISOU 2638 O MET A 365 6456 5732 8044 -874 2889 1510 A O ATOM 2639 CB MET A 365 -36.291 23.337 32.597 1.00 54.25 A C ANISOU 2639 CB MET A 365 7236 5701 7674 -766 2604 1457 A C ATOM 2640 CG MET A 365 -37.540 22.713 33.186 1.00 54.44 A C ANISOU 2640 CG MET A 365 7276 5731 7677 -639 2447 1475 A C ATOM 2641 SD MET A 365 -38.843 22.505 31.959 1.00 53.97 A S ANISOU 2641 SD MET A 365 7635 5519 7351 -577 2454 1379 A S ATOM 2642 CE MET A 365 -37.925 21.770 30.604 1.00 60.67 A C ANISOU 2642 CE MET A 365 8529 6298 8226 -591 2755 1298 A C ATOM 2643 N ARG A 366 -33.616 25.047 32.391 1.00 51.43 A N ANISOU 2643 N ARG A 366 6680 5426 7435 -1076 2790 1488 A N ATOM 2644 CA ARG A 366 -32.325 25.289 31.757 1.00 56.55 A C ANISOU 2644 CA ARG A 366 7255 6081 8152 -1183 2987 1463 A C ATOM 2645 C ARG A 366 -31.201 25.302 32.785 1.00 58.42 A C ANISOU 2645 C ARG A 366 7108 6449 8639 -1227 2951 1538 A C ATOM 2646 O ARG A 366 -30.144 24.700 32.565 1.00 59.79 A O ANISOU 2646 O ARG A 366 7060 6651 9007 -1215 3117 1522 A O ATOM 2647 CB ARG A 366 -32.351 26.609 30.984 1.00 61.45 A C ANISOU 2647 CB ARG A 366 8190 6627 8530 -1339 2995 1435 A C ATOM 2648 CG ARG A 366 -32.888 26.515 29.563 1.00 64.55 A C ANISOU 2648 CG ARG A 366 8942 6882 8703 -1333 3116 1339 A C ATOM 2649 CD ARG A 366 -32.611 27.799 28.792 1.00 69.14 A C ANISOU 2649 CD ARG A 366 9791 7396 9083 -1502 3138 1319 A C ATOM 2650 NE ARG A 366 -33.270 28.949 29.404 1.00 71.41 A N ANISOU 2650 NE ARG A 366 10220 7668 9244 -1552 2891 1373 A N ATOM 2651 CZ ARG A 366 -34.494 29.358 29.090 1.00 71.56 A C ANISOU 2651 CZ ARG A 366 10563 7580 9046 -1511 2730 1346 A C ATOM 2652 NH1 ARG A 366 -35.190 28.708 28.166 1.00 71.18 A N1+ ANISOU 2652 NH1 ARG A 366 10731 7442 8873 -1431 2781 1273 A N1+ ATOM 2653 NH2 ARG A 366 -35.023 30.413 29.698 1.00 69.40 A N ANISOU 2653 NH2 ARG A 366 10400 7284 8687 -1548 2511 1387 A N ATOM 2654 N HIS A 367 -31.414 25.977 33.917 1.00 59.08 A N ANISOU 2654 N HIS A 367 7115 6608 8725 -1278 2730 1615 A N ATOM 2655 CA HIS A 367 -30.375 26.074 34.938 1.00 61.28 A C ANISOU 2655 CA HIS A 367 7055 7011 9216 -1338 2659 1687 A C ATOM 2656 C HIS A 367 -30.076 24.712 35.549 1.00 58.81 A C ANISOU 2656 C HIS A 367 6425 6757 9163 -1187 2648 1718 A C ATOM 2657 O HIS A 367 -28.913 24.303 35.643 1.00 60.25 A O ANISOU 2657 O HIS A 367 6341 6986 9565 -1190 2736 1732 A O ATOM 2658 CB HIS A 367 -30.809 27.059 36.023 1.00 64.76 A C ANISOU 2658 CB HIS A 367 7524 7505 9575 -1427 2415 1753 A C ATOM 2659 CG HIS A 367 -29.732 27.391 37.009 1.00 67.95 A C ANISOU 2659 CG HIS A 367 7642 8029 10146 -1530 2327 1818 A C ATOM 2660 CD2 HIS A 367 -29.334 26.767 38.144 1.00 67.69 A C ANISOU 2660 CD2 HIS A 367 7302 8100 10319 -1477 2193 1881 A C ATOM 2661 ND1 HIS A 367 -28.926 28.501 36.880 1.00 69.73 A N ANISOU 2661 ND1 HIS A 367 7898 8271 10325 -1719 2358 1827 A N ATOM 2662 CE1 HIS A 367 -28.078 28.547 37.892 1.00 70.55 A C ANISOU 2662 CE1 HIS A 367 7722 8485 10600 -1778 2255 1884 A C ATOM 2663 NE2 HIS A 367 -28.302 27.505 38.671 1.00 69.51 A N ANISOU 2663 NE2 HIS A 367 7385 8405 10622 -1629 2146 1919 A N ATOM 2664 N ILE A 368 -31.118 23.998 35.974 1.00 51.98 A N ANISOU 2664 N ILE A 368 5585 5883 8283 -1051 2532 1732 A N ATOM 2665 CA ILE A 368 -30.923 22.698 36.607 1.00 54.23 A C ANISOU 2665 CA ILE A 368 5591 6210 8803 -908 2490 1775 A C ATOM 2666 C ILE A 368 -30.182 21.757 35.666 1.00 61.39 A C ANISOU 2666 C ILE A 368 6413 7049 9865 -828 2742 1717 A C ATOM 2667 O ILE A 368 -29.213 21.093 36.054 1.00 68.25 A O ANISOU 2667 O ILE A 368 6985 7953 10995 -780 2764 1755 A O ATOM 2668 CB ILE A 368 -32.273 22.108 37.048 1.00 49.64 A C ANISOU 2668 CB ILE A 368 5100 5619 8142 -790 2346 1789 A C ATOM 2669 CG1 ILE A 368 -32.839 22.904 38.228 1.00 46.12 A C ANISOU 2669 CG1 ILE A 368 4659 5258 7605 -864 2086 1852 A C ATOM 2670 CG2 ILE A 368 -32.116 20.633 37.386 1.00 49.54 A C ANISOU 2670 CG2 ILE A 368 4857 5611 8353 -636 2349 1823 A C ATOM 2671 CD1 ILE A 368 -34.298 22.616 38.518 1.00 44.65 A C ANISOU 2671 CD1 ILE A 368 4622 5057 7285 -781 1961 1848 A C ATOM 2672 N GLN A 369 -30.631 21.686 34.411 1.00 63.98 A N ANISOU 2672 N GLN A 369 7011 7267 10033 -813 2929 1621 A N ATOM 2673 CA GLN A 369 -30.017 20.765 33.460 1.00 67.89 A C ANISOU 2673 CA GLN A 369 7459 7681 10655 -739 3185 1546 A C ATOM 2674 C GLN A 369 -28.540 21.079 33.251 1.00 73.34 A C ANISOU 2674 C GLN A 369 7953 8404 11509 -832 3329 1537 A C ATOM 2675 O GLN A 369 -27.704 20.168 33.209 1.00 75.08 A O ANISOU 2675 O GLN A 369 7931 8608 11987 -747 3446 1529 A O ATOM 2676 CB GLN A 369 -30.768 20.798 32.129 1.00 66.44 A C ANISOU 2676 CB GLN A 369 7647 7373 10223 -742 3346 1439 A C ATOM 2677 CG GLN A 369 -30.252 19.796 31.098 1.00 67.91 A C ANISOU 2677 CG GLN A 369 7827 7459 10514 -670 3622 1344 A C ATOM 2678 CD GLN A 369 -30.237 18.366 31.616 1.00 66.63 A C ANISOU 2678 CD GLN A 369 7424 7284 10607 -492 3611 1373 A C ATOM 2679 NE2 GLN A 369 -29.322 18.074 32.530 1.00 67.69 A N ANISOU 2679 NE2 GLN A 369 7201 7494 11024 -460 3537 1454 A N ATOM 2680 OE1 GLN A 369 -31.035 17.533 31.191 1.00 63.67 A O ANISOU 2680 OE1 GLN A 369 7194 6825 10175 -389 3658 1328 A O ATOM 2681 N GLU A 370 -28.200 22.362 33.112 1.00 82.35 A N ANISOU 2681 N GLU A 370 9196 9584 12510 -1007 3321 1539 A N ATOM 2682 CA GLU A 370 -26.820 22.728 32.809 1.00 87.25 A C ANISOU 2682 CA GLU A 370 9652 10238 13262 -1116 3475 1523 A C ATOM 2683 C GLU A 370 -25.877 22.438 33.970 1.00 88.21 A C ANISOU 2683 C GLU A 370 9370 10464 13680 -1094 3348 1613 A C ATOM 2684 O GLU A 370 -24.707 22.108 33.746 1.00 92.02 A O ANISOU 2684 O GLU A 370 9626 10955 14381 -1098 3497 1594 A O ATOM 2685 CB GLU A 370 -26.745 24.207 32.431 1.00 89.25 A C ANISOU 2685 CB GLU A 370 10127 10505 13280 -1320 3474 1516 A C ATOM 2686 N HIS A 371 -26.357 22.552 35.206 1.00 85.70 A N ANISOU 2686 N HIS A 371 8966 10222 13373 -1075 3071 1710 A N ATOM 2687 CA HIS A 371 -25.531 22.357 36.390 1.00 83.92 A C ANISOU 2687 CA HIS A 371 8395 10094 13396 -1070 2904 1807 A C ATOM 2688 C HIS A 371 -25.700 20.977 37.016 1.00 80.15 A C ANISOU 2688 C HIS A 371 7717 9598 13137 -876 2807 1861 A C ATOM 2689 O HIS A 371 -25.368 20.793 38.192 1.00 79.39 A O ANISOU 2689 O HIS A 371 7393 9576 13195 -862 2588 1964 A O ATOM 2690 CB HIS A 371 -25.825 23.452 37.412 1.00 84.59 A C ANISOU 2690 CB HIS A 371 8520 10273 13346 -1204 2650 1880 A C ATOM 2691 CG HIS A 371 -25.457 24.821 36.937 1.00 88.63 A C ANISOU 2691 CG HIS A 371 9189 10802 13686 -1409 2723 1846 A C ATOM 2692 CD2 HIS A 371 -24.355 25.272 36.293 1.00 92.09 A C ANISOU 2692 CD2 HIS A 371 9562 11249 14179 -1528 2906 1810 A C ATOM 2693 ND1 HIS A 371 -26.282 25.913 37.096 1.00 87.57 A N ANISOU 2693 ND1 HIS A 371 9319 10665 13288 -1521 2602 1852 A N ATOM 2694 CE1 HIS A 371 -25.700 26.979 36.577 1.00 89.35 A C ANISOU 2694 CE1 HIS A 371 9647 10893 13411 -1702 2697 1829 A C ATOM 2695 NE2 HIS A 371 -24.529 26.618 36.084 1.00 91.84 A N ANISOU 2695 NE2 HIS A 371 9762 11223 13909 -1716 2884 1804 A N ATOM 2696 N TYR A 372 -26.205 20.007 36.261 1.00 77.00 A N ANISOU 2696 N TYR A 372 7415 9094 12747 -736 2959 1798 A N ATOM 2697 CA TYR A 372 -26.418 18.652 36.749 1.00 74.56 A C ANISOU 2697 CA TYR A 372 6947 8746 12637 -556 2883 1848 A C ATOM 2698 C TYR A 372 -25.521 17.696 35.976 1.00 76.92 A C ANISOU 2698 C TYR A 372 7097 8946 13181 -459 3130 1786 A C ATOM 2699 O TYR A 372 -25.542 17.681 34.741 1.00 77.19 A O ANISOU 2699 O TYR A 372 7311 8895 13121 -468 3394 1666 A O ATOM 2700 CB TYR A 372 -27.892 18.256 36.612 1.00 68.65 A C ANISOU 2700 CB TYR A 372 6444 7948 11690 -471 2833 1827 A C ATOM 2701 CG TYR A 372 -28.190 16.795 36.860 1.00 67.96 A C ANISOU 2701 CG TYR A 372 6245 7795 11780 -291 2805 1860 A C ATOM 2702 CD1 TYR A 372 -27.927 16.209 38.091 1.00 67.15 A C ANISOU 2702 CD1 TYR A 372 5891 7745 11880 -234 2575 1987 A C ATOM 2703 CD2 TYR A 372 -28.762 16.008 35.868 1.00 67.26 A C ANISOU 2703 CD2 TYR A 372 6328 7585 11642 -191 3000 1768 A C ATOM 2704 CE1 TYR A 372 -28.207 14.874 38.320 1.00 66.35 A C ANISOU 2704 CE1 TYR A 372 5703 7570 11936 -80 2541 2028 A C ATOM 2705 CE2 TYR A 372 -29.046 14.674 36.087 1.00 65.63 A C ANISOU 2705 CE2 TYR A 372 6032 7309 11595 -35 2978 1800 A C ATOM 2706 CZ TYR A 372 -28.767 14.112 37.314 1.00 64.64 A C ANISOU 2706 CZ TYR A 372 5649 7232 11678 20 2747 1933 A C ATOM 2707 OH TYR A 372 -29.050 12.784 37.539 1.00 62.25 A O ANISOU 2707 OH TYR A 372 5270 6849 11532 163 2716 1974 A O ATOM 2708 N GLY A 373 -24.742 16.896 36.706 1.00 81.11 A N ANISOU 2708 N GLY A 373 7316 9481 14023 -371 3038 1868 A N ATOM 2709 CA GLY A 373 -23.837 15.946 36.088 1.00 88.14 A C ANISOU 2709 CA GLY A 373 8033 10267 15187 -270 3255 1815 A C ATOM 2710 C GLY A 373 -24.535 14.711 35.561 1.00 92.76 A C ANISOU 2710 C GLY A 373 8726 10718 15803 -108 3363 1766 A C ATOM 2711 O GLY A 373 -24.256 13.581 35.978 1.00 95.25 A O ANISOU 2711 O GLY A 373 8847 10966 16378 28 3311 1821 A O ATOM 2712 N GLY A 374 -25.449 14.935 34.631 1.00 93.78 A N ANISOU 2712 N GLY A 374 9178 10798 15657 -129 3509 1662 A N ATOM 2713 CA GLY A 374 -26.233 13.868 34.046 1.00 92.32 A C ANISOU 2713 CA GLY A 374 9146 10485 15446 2 3619 1603 A C ATOM 2714 C GLY A 374 -27.351 14.472 33.234 1.00 92.38 A C ANISOU 2714 C GLY A 374 9536 10476 15088 -65 3696 1514 A C ATOM 2715 O GLY A 374 -27.558 15.687 33.218 1.00 93.27 A O ANISOU 2715 O GLY A 374 9788 10671 14978 -204 3640 1513 A O ATOM 2716 N THR A 375 -28.080 13.600 32.553 1.00 91.13 A N ANISOU 2716 N THR A 375 9558 10199 14867 32 3819 1442 A N ATOM 2717 CA THR A 375 -29.235 14.024 31.778 1.00 89.39 A C ANISOU 2717 CA THR A 375 9717 9946 14301 -18 3871 1363 A C ATOM 2718 C THR A 375 -30.476 13.957 32.656 1.00 84.81 A C ANISOU 2718 C THR A 375 9199 9428 13598 27 3605 1452 A C ATOM 2719 O THR A 375 -30.743 12.927 33.285 1.00 84.94 A O ANISOU 2719 O THR A 375 9075 9424 13774 151 3504 1517 A O ATOM 2720 CB THR A 375 -29.413 13.160 30.532 1.00 90.45 A C ANISOU 2720 CB THR A 375 10048 9919 14401 43 4143 1229 A C ATOM 2721 CG2 THR A 375 -30.716 13.514 29.839 1.00 87.80 A C ANISOU 2721 CG2 THR A 375 10112 9547 13703 -1 4146 1164 A C ATOM 2722 OG1 THR A 375 -28.319 13.384 29.634 1.00 94.68 A O ANISOU 2722 OG1 THR A 375 10567 10404 15003 -30 4404 1129 A O ATOM 2723 N ALA A 376 -31.241 15.047 32.675 1.00 80.34 A N ANISOU 2723 N ALA A 376 8851 8928 12749 -78 3495 1453 A N ATOM 2724 CA ALA A 376 -32.400 15.187 33.544 1.00 75.42 A C ANISOU 2724 CA ALA A 376 8285 8376 11994 -61 3237 1531 A C ATOM 2725 C ALA A 376 -33.666 15.324 32.713 1.00 72.58 A C ANISOU 2725 C ALA A 376 8298 7947 11331 -69 3280 1449 A C ATOM 2726 O ALA A 376 -33.656 15.946 31.648 1.00 71.94 A O ANISOU 2726 O ALA A 376 8469 7805 11061 -153 3430 1355 A O ATOM 2727 CB ALA A 376 -32.249 16.399 34.474 1.00 75.59 A C ANISOU 2727 CB ALA A 376 8227 8534 11959 -181 3024 1612 A C ATOM 2728 N THR A 377 -34.752 14.732 33.204 1.00 69.03 A N ANISOU 2728 N THR A 377 7891 7505 10832 11 3136 1487 A N ATOM 2729 CA THR A 377 -36.063 14.827 32.581 1.00 63.80 A C ANISOU 2729 CA THR A 377 7567 6785 9888 10 3124 1425 A C ATOM 2730 C THR A 377 -36.975 15.701 33.435 1.00 60.76 A C ANISOU 2730 C THR A 377 7243 6498 9345 -43 2861 1489 A C ATOM 2731 O THR A 377 -36.877 15.713 34.665 1.00 62.56 A O ANISOU 2731 O THR A 377 7234 6836 9700 -38 2674 1588 A O ATOM 2732 CB THR A 377 -36.693 13.439 32.396 1.00 59.92 A C ANISOU 2732 CB THR A 377 7103 6214 9448 138 3177 1406 A C ATOM 2733 CG2 THR A 377 -37.921 13.520 31.497 1.00 57.78 A C ANISOU 2733 CG2 THR A 377 7217 5860 8875 125 3196 1321 A C ATOM 2734 OG1 THR A 377 -35.738 12.549 31.805 1.00 60.69 A O ANISOU 2734 OG1 THR A 377 7090 6216 9753 200 3410 1355 A O ATOM 2735 N PHE A 378 -37.867 16.436 32.774 1.00 57.70 A N ANISOU 2735 N PHE A 378 7188 6061 8676 -97 2836 1428 A N ATOM 2736 CA PHE A 378 -38.736 17.392 33.448 1.00 57.14 A C ANISOU 2736 CA PHE A 378 7210 6054 8447 -147 2600 1467 A C ATOM 2737 C PHE A 378 -40.197 17.105 33.140 1.00 59.26 A C ANISOU 2737 C PHE A 378 7730 6284 8501 -75 2453 1387 A C ATOM 2738 O PHE A 378 -40.549 16.749 32.012 1.00 61.92 A O ANISOU 2738 O PHE A 378 8312 6505 8712 -57 2581 1309 A O ATOM 2739 CB PHE A 378 -38.397 18.837 33.051 1.00 55.94 A C ANISOU 2739 CB PHE A 378 7216 5889 8148 -279 2607 1445 A C ATOM 2740 CG PHE A 378 -36.989 19.237 33.380 1.00 55.49 A C ANISOU 2740 CG PHE A 378 6915 5902 8269 -354 2675 1484 A C ATOM 2741 CD1 PHE A 378 -36.633 19.543 34.683 1.00 53.56 A C ANISOU 2741 CD1 PHE A 378 6405 5782 8163 -383 2506 1580 A C ATOM 2742 CD2 PHE A 378 -36.021 19.299 32.393 1.00 55.69 A C ANISOU 2742 CD2 PHE A 378 6977 5866 8317 -405 2902 1421 A C ATOM 2743 CE1 PHE A 378 -35.339 19.905 34.996 1.00 53.43 A C ANISOU 2743 CE1 PHE A 378 6167 5828 8307 -457 2547 1616 A C ATOM 2744 CE2 PHE A 378 -34.724 19.662 32.700 1.00 55.90 A C ANISOU 2744 CE2 PHE A 378 6769 5957 8515 -476 2959 1455 A C ATOM 2745 CZ PHE A 378 -34.383 19.966 34.004 1.00 56.15 A C ANISOU 2745 CZ PHE A 378 6537 6111 8685 -500 2774 1555 A C ATOM 2746 N TYR A 379 -41.041 17.267 34.158 1.00 55.99 A N ANISOU 2746 N TYR A 379 7255 5970 8048 -45 2184 1403 A N ATOM 2747 CA TYR A 379 -42.489 17.208 34.008 1.00 50.79 A C ANISOU 2747 CA TYR A 379 6806 5296 7195 11 2009 1324 A C ATOM 2748 C TYR A 379 -43.078 18.438 34.679 1.00 47.03 A C ANISOU 2748 C TYR A 379 6376 4891 6601 -37 1779 1314 A C ATOM 2749 O TYR A 379 -42.908 18.628 35.888 1.00 48.94 A O ANISOU 2749 O TYR A 379 6399 5254 6941 -58 1653 1371 A O ATOM 2750 CB TYR A 379 -43.077 15.940 34.639 1.00 47.62 A C ANISOU 2750 CB TYR A 379 6265 4946 6883 108 1921 1334 A C ATOM 2751 CG TYR A 379 -42.415 14.636 34.250 1.00 48.94 A C ANISOU 2751 CG TYR A 379 6327 5048 7220 167 2127 1357 A C ATOM 2752 CD1 TYR A 379 -42.760 13.974 33.077 1.00 50.47 A C ANISOU 2752 CD1 TYR A 379 6739 5113 7323 208 2271 1278 A C ATOM 2753 CD2 TYR A 379 -41.466 14.051 35.077 1.00 49.02 A C ANISOU 2753 CD2 TYR A 379 6023 5117 7487 183 2164 1458 A C ATOM 2754 CE1 TYR A 379 -42.162 12.776 32.733 1.00 50.87 A C ANISOU 2754 CE1 TYR A 379 6699 5092 7538 267 2469 1286 A C ATOM 2755 CE2 TYR A 379 -40.866 12.859 34.744 1.00 50.72 A C ANISOU 2755 CE2 TYR A 379 6130 5256 7884 253 2344 1475 A C ATOM 2756 CZ TYR A 379 -41.215 12.224 33.573 1.00 52.37 A C ANISOU 2756 CZ TYR A 379 6560 5334 8003 298 2507 1383 A C ATOM 2757 OH TYR A 379 -40.607 11.033 33.249 1.00 53.25 A O ANISOU 2757 OH TYR A 379 6568 5358 8308 372 2698 1387 A O ATOM 2758 N LEU A 380 -43.764 19.269 33.900 1.00 45.92 A N ANISOU 2758 N LEU A 380 6527 4667 6253 -57 1722 1240 A N ATOM 2759 CA LEU A 380 -44.558 20.367 34.447 1.00 44.92 A C ANISOU 2759 CA LEU A 380 6473 4582 6014 -74 1489 1204 A C ATOM 2760 C LEU A 380 -45.967 19.824 34.617 1.00 47.43 A C ANISOU 2760 C LEU A 380 6841 4920 6260 23 1317 1130 A C ATOM 2761 O LEU A 380 -46.713 19.677 33.645 1.00 50.85 A O ANISOU 2761 O LEU A 380 7511 5252 6559 61 1302 1063 A O ATOM 2762 CB LEU A 380 -44.536 21.586 33.532 1.00 46.28 A C ANISOU 2762 CB LEU A 380 6929 4635 6018 -145 1497 1171 A C ATOM 2763 CG LEU A 380 -43.331 22.528 33.557 1.00 50.02 A C ANISOU 2763 CG LEU A 380 7371 5103 6531 -268 1606 1233 A C ATOM 2764 CD1 LEU A 380 -43.479 23.571 32.463 1.00 49.29 A C ANISOU 2764 CD1 LEU A 380 7624 4865 6240 -338 1613 1195 A C ATOM 2765 CD2 LEU A 380 -43.179 23.196 34.918 1.00 49.85 A C ANISOU 2765 CD2 LEU A 380 7139 5207 6593 -304 1453 1271 A C ATOM 2766 N SER A 381 -46.337 19.525 35.854 1.00 43.80 A N ANISOU 2766 N SER A 381 6164 4593 5884 48 1183 1142 A N ATOM 2767 CA SER A 381 -47.576 18.820 36.122 1.00 44.59 A C ANISOU 2767 CA SER A 381 6261 4732 5948 126 1050 1077 A C ATOM 2768 C SER A 381 -48.496 19.649 37.004 1.00 41.44 A C ANISOU 2768 C SER A 381 5834 4416 5495 126 835 1012 A C ATOM 2769 O SER A 381 -48.051 20.421 37.858 1.00 42.41 A O ANISOU 2769 O SER A 381 5846 4612 5657 64 787 1043 A O ATOM 2770 CB SER A 381 -47.306 17.469 36.796 1.00 47.09 A C ANISOU 2770 CB SER A 381 6350 5129 6412 153 1102 1138 A C ATOM 2771 OG SER A 381 -48.500 16.719 36.939 1.00 49.07 A O ANISOU 2771 OG SER A 381 6619 5407 6617 215 994 1073 A O ATOM 2772 N GLN A 382 -49.789 19.468 36.774 1.00 40.43 A N ANISOU 2772 N GLN A 382 5807 4272 5283 194 709 916 A N ATOM 2773 CA GLN A 382 -50.849 19.963 37.631 1.00 40.38 A C ANISOU 2773 CA GLN A 382 5740 4351 5252 213 520 830 A C ATOM 2774 C GLN A 382 -51.380 18.809 38.467 1.00 40.66 A C ANISOU 2774 C GLN A 382 5591 4507 5352 230 489 825 A C ATOM 2775 O GLN A 382 -51.125 17.637 38.178 1.00 41.80 A O ANISOU 2775 O GLN A 382 5703 4638 5543 248 588 876 A O ATOM 2776 CB GLN A 382 -51.985 20.570 36.803 1.00 45.56 A C ANISOU 2776 CB GLN A 382 6616 4905 5791 277 387 720 A C ATOM 2777 CG GLN A 382 -51.564 21.685 35.856 1.00 53.20 A C ANISOU 2777 CG GLN A 382 7817 5728 6670 253 397 729 A C ATOM 2778 CD GLN A 382 -52.703 22.146 34.959 1.00 59.52 A C ANISOU 2778 CD GLN A 382 8847 6407 7360 320 241 637 A C ATOM 2779 NE2 GLN A 382 -52.651 23.406 34.537 1.00 62.60 A N ANISOU 2779 NE2 GLN A 382 9415 6690 7681 304 164 623 A N ATOM 2780 OE1 GLN A 382 -53.618 21.380 34.652 1.00 60.99 A O ANISOU 2780 OE1 GLN A 382 9054 6592 7529 381 178 583 A O ATOM 2781 N ALA A 383 -52.126 19.147 39.512 1.00 37.06 A N ANISOU 2781 N ALA A 383 5024 4162 4897 217 358 757 A N ATOM 2782 CA ALA A 383 -52.767 18.108 40.300 1.00 37.71 A C ANISOU 2782 CA ALA A 383 4956 4358 5016 215 321 739 A C ATOM 2783 C ALA A 383 -53.816 17.420 39.437 1.00 36.30 A C ANISOU 2783 C ALA A 383 4891 4116 4786 293 286 663 A C ATOM 2784 O ALA A 383 -54.662 18.082 38.830 1.00 40.10 A O ANISOU 2784 O ALA A 383 5507 4530 5199 347 187 562 A O ATOM 2785 CB ALA A 383 -53.400 18.704 41.555 1.00 40.18 A C ANISOU 2785 CB ALA A 383 5146 4800 5322 169 206 661 A C ATOM 2786 N ALA A 384 -53.764 16.095 39.377 1.00 33.60 A N ANISOU 2786 N ALA A 384 4498 3786 4482 297 355 712 A N ATOM 2787 CA ALA A 384 -54.598 15.334 38.460 1.00 32.54 A C ANISOU 2787 CA ALA A 384 4488 3578 4298 356 339 655 A C ATOM 2788 C ALA A 384 -55.612 14.495 39.225 1.00 33.21 A C ANISOU 2788 C ALA A 384 4446 3775 4398 341 262 600 A C ATOM 2789 O ALA A 384 -55.589 14.405 40.454 1.00 37.29 A O ANISOU 2789 O ALA A 384 4788 4423 4957 278 238 616 A O ATOM 2790 CB ALA A 384 -53.739 14.437 37.563 1.00 33.61 A C ANISOU 2790 CB ALA A 384 4710 3604 4457 370 501 743 A C ATOM 2791 N ASP A 385 -56.515 13.877 38.468 1.00 35.06 A N ANISOU 2791 N ASP A 385 4783 3954 4584 385 221 534 A N ATOM 2792 CA ASP A 385 -57.525 13.009 39.047 1.00 35.04 A C ANISOU 2792 CA ASP A 385 4676 4047 4590 362 156 477 A C ATOM 2793 C ASP A 385 -56.940 11.643 39.393 1.00 33.92 A C ANISOU 2793 C ASP A 385 4460 3923 4506 321 260 583 A C ATOM 2794 O ASP A 385 -55.908 11.222 38.862 1.00 35.23 A O ANISOU 2794 O ASP A 385 4682 3994 4708 338 385 682 A O ATOM 2795 CB ASP A 385 -58.707 12.840 38.092 1.00 41.16 A C ANISOU 2795 CB ASP A 385 5585 4752 5301 415 60 370 A C ATOM 2796 CG ASP A 385 -59.599 14.062 38.047 1.00 47.96 A C ANISOU 2796 CG ASP A 385 6461 5622 6139 458 -91 247 A C ATOM 2797 OD1 ASP A 385 -59.957 14.566 39.132 1.00 49.79 A O ANISOU 2797 OD1 ASP A 385 6529 5978 6411 428 -140 187 A O ATOM 2798 OD2 ASP A 385 -59.962 14.506 36.936 1.00 52.09 A O1- ANISOU 2798 OD2 ASP A 385 7166 6020 6604 517 -165 206 A O1- ATOM 2799 N GLY A 386 -57.625 10.950 40.297 1.00 31.58 A N ANISOU 2799 N GLY A 386 4034 3741 4223 263 210 558 A N ATOM 2800 CA GLY A 386 -57.275 9.596 40.656 1.00 36.11 A C ANISOU 2800 CA GLY A 386 4550 4323 4848 220 276 653 A C ATOM 2801 C GLY A 386 -57.844 8.582 39.681 1.00 34.77 A C ANISOU 2801 C GLY A 386 4510 4054 4646 256 292 621 A C ATOM 2802 O GLY A 386 -58.303 8.902 38.583 1.00 39.96 A O ANISOU 2802 O GLY A 386 5324 4618 5239 315 267 547 A O ATOM 2803 N ALA A 387 -57.810 7.323 40.113 1.00 34.66 A N ANISOU 2803 N ALA A 387 4443 4054 4672 209 324 683 A N ATOM 2804 CA ALA A 387 -58.266 6.223 39.275 1.00 38.29 A C ANISOU 2804 CA ALA A 387 5028 4414 5107 228 350 663 A C ATOM 2805 C ALA A 387 -59.694 6.456 38.798 1.00 38.09 A C ANISOU 2805 C ALA A 387 5070 4412 4992 230 231 516 A C ATOM 2806 O ALA A 387 -60.541 6.966 39.537 1.00 42.09 A O ANISOU 2806 O ALA A 387 5460 5052 5482 187 130 432 A O ATOM 2807 CB ALA A 387 -58.181 4.904 40.045 1.00 38.85 A C ANISOU 2807 CB ALA A 387 5014 4513 5233 159 370 744 A C ATOM 2808 N LYS A 388 -59.953 6.082 37.548 1.00 39.95 A N ANISOU 2808 N LYS A 388 5493 4514 5173 276 245 480 A N ATOM 2809 CA LYS A 388 -61.285 6.189 36.974 1.00 41.02 A C ANISOU 2809 CA LYS A 388 5701 4651 5232 277 115 352 A C ATOM 2810 C LYS A 388 -61.434 5.130 35.893 1.00 44.19 A C ANISOU 2810 C LYS A 388 6295 4911 5583 281 156 353 A C ATOM 2811 O LYS A 388 -60.449 4.660 35.317 1.00 46.24 A O ANISOU 2811 O LYS A 388 6669 5044 5854 310 298 431 A O ATOM 2812 CB LYS A 388 -61.539 7.587 36.395 1.00 39.93 A C ANISOU 2812 CB LYS A 388 5635 4487 5050 340 25 279 A C ATOM 2813 CG LYS A 388 -60.634 7.944 35.224 1.00 41.22 A C ANISOU 2813 CG LYS A 388 6012 4485 5165 398 113 330 A C ATOM 2814 CD LYS A 388 -60.951 9.322 34.678 1.00 44.47 A C ANISOU 2814 CD LYS A 388 6514 4861 5523 447 -0 266 A C ATOM 2815 CE LYS A 388 -60.590 10.389 35.692 1.00 47.63 A C ANISOU 2815 CE LYS A 388 6743 5368 5986 452 -15 273 A C ATOM 2816 NZ LYS A 388 -60.494 11.741 35.083 1.00 50.57 A N1+ ANISOU 2816 NZ LYS A 388 7237 5664 6312 503 -83 245 A N1+ ATOM 2817 N VAL A 389 -62.683 4.770 35.617 1.00 45.79 A N ANISOU 2817 N VAL A 389 6527 5135 5735 247 34 257 A N ATOM 2818 CA VAL A 389 -63.003 3.859 34.525 1.00 43.29 A C ANISOU 2818 CA VAL A 389 6415 4684 5348 237 43 238 A C ATOM 2819 C VAL A 389 -63.072 4.641 33.220 1.00 45.72 A C ANISOU 2819 C VAL A 389 6943 4866 5561 293 -8 194 A C ATOM 2820 O VAL A 389 -63.497 5.801 33.187 1.00 46.40 A O ANISOU 2820 O VAL A 389 7000 4995 5635 329 -132 138 A O ATOM 2821 CB VAL A 389 -64.320 3.109 34.808 1.00 43.56 A C ANISOU 2821 CB VAL A 389 6382 4797 5370 158 -76 159 A C ATOM 2822 CG1 VAL A 389 -64.597 2.090 33.713 1.00 40.68 A C ANISOU 2822 CG1 VAL A 389 6241 4288 4928 132 -65 145 A C ATOM 2823 CG2 VAL A 389 -64.264 2.435 36.176 1.00 47.63 A C ANISOU 2823 CG2 VAL A 389 6692 5443 5961 80 -31 206 A C ATOM 2824 N LEU A 390 -62.660 4.005 32.129 1.00 45.52 A N ANISOU 2824 N LEU A 390 7154 4677 5464 294 86 217 A N ATOM 2825 CA LEU A 390 -62.722 4.607 30.802 1.00 46.62 A C ANISOU 2825 CA LEU A 390 7553 4680 5480 318 43 181 A C ATOM 2826 C LEU A 390 -63.724 3.828 29.963 1.00 50.64 A C ANISOU 2826 C LEU A 390 8234 5116 5891 264 -63 114 A C ATOM 2827 O LEU A 390 -63.577 2.613 29.788 1.00 53.23 A O ANISOU 2827 O LEU A 390 8634 5379 6210 222 42 132 A O ATOM 2828 CB LEU A 390 -61.349 4.600 30.130 1.00 43.65 A C ANISOU 2828 CB LEU A 390 7343 4163 5079 345 261 253 A C ATOM 2829 CG LEU A 390 -60.174 5.259 30.851 1.00 39.35 A C ANISOU 2829 CG LEU A 390 6642 3671 4638 388 390 333 A C ATOM 2830 CD1 LEU A 390 -58.909 5.080 30.031 1.00 38.98 A C ANISOU 2830 CD1 LEU A 390 6767 3473 4573 402 620 386 A C ATOM 2831 CD2 LEU A 390 -60.449 6.736 31.108 1.00 40.48 A C ANISOU 2831 CD2 LEU A 390 6720 3889 4770 417 248 305 A C ATOM 2832 N CYS A 391 -64.741 4.521 29.451 1.00 50.63 A N ANISOU 2832 N CYS A 391 8296 5116 5823 265 -281 38 A N ATOM 2833 CA CYS A 391 -65.788 3.856 28.685 1.00 49.69 A C ANISOU 2833 CA CYS A 391 8325 4939 5616 203 -421 -28 A C ATOM 2834 C CYS A 391 -65.339 3.724 27.236 1.00 50.68 A C ANISOU 2834 C CYS A 391 8817 4862 5578 180 -361 -13 A C ATOM 2835 O CYS A 391 -65.018 4.726 26.589 1.00 50.50 A O ANISOU 2835 O CYS A 391 8947 4763 5479 211 -394 -2 A O ATOM 2836 CB CYS A 391 -67.099 4.636 28.763 1.00 52.03 A C ANISOU 2836 CB CYS A 391 8514 5321 5935 215 -701 -116 A C ATOM 2837 SG CYS A 391 -67.837 4.833 30.417 1.00 58.61 A S ANISOU 2837 SG CYS A 391 8923 6399 6949 221 -771 -171 A S ATOM 2838 N LEU A 392 -65.325 2.497 26.726 1.00 52.51 A N ANISOU 2838 N LEU A 392 9207 4999 5745 114 -269 -17 A N ATOM 2839 CA LEU A 392 -64.950 2.259 25.336 1.00 57.78 A C ANISOU 2839 CA LEU A 392 10245 5468 6239 70 -193 -19 A C ATOM 2840 C LEU A 392 -66.178 2.175 24.428 1.00 65.06 A C ANISOU 2840 C LEU A 392 11362 6332 7025 -5 -444 -88 A C ATOM 2841 O LEU A 392 -67.209 1.596 24.783 1.00 66.50 A O ANISOU 2841 O LEU A 392 11421 6594 7251 -48 -594 -135 A O ATOM 2842 CB LEU A 392 -64.113 0.986 25.217 1.00 53.04 A C ANISOU 2842 CB LEU A 392 9735 4770 5647 43 75 9 A C ATOM 2843 CG LEU A 392 -62.726 1.052 25.854 1.00 49.54 A C ANISOU 2843 CG LEU A 392 9150 4339 5334 116 333 85 A C ATOM 2844 CD1 LEU A 392 -62.049 -0.303 25.801 1.00 49.60 A C ANISOU 2844 CD1 LEU A 392 9214 4243 5387 102 567 105 A C ATOM 2845 CD2 LEU A 392 -61.877 2.106 25.164 1.00 49.24 A C ANISOU 2845 CD2 LEU A 392 9270 4220 5220 145 425 107 A C ATOM 2846 OXT LEU A 392 -66.161 2.686 23.307 1.00 67.73 A O1- ANISOU 2846 OXT LEU A 392 11993 6540 7203 -35 -509 -95 A O1- TER HETATM 2847 O HOH A 501 -60.676 -1.174 18.169 1.00 44.28 DA O HETATM 2848 O HOH A 502 -29.034 30.402 35.337 1.00 53.09 DA O HETATM 2849 O HOH A 503 -60.659 1.856 41.444 1.00 30.99 DA O HETATM 2850 O HOH A 504 -45.772 32.839 37.025 1.00 41.38 DA O HETATM 2851 O HOH A 505 -37.858 31.418 32.829 1.00 36.28 DA O HETATM 2852 O HOH A 506 -26.441 15.325 67.328 1.00 51.55 DA O HETATM 2853 O HOH A 507 -60.873 -17.308 26.328 1.00 39.24 DA O HETATM 2854 O HOH A 508 -50.138 24.287 39.621 1.00 51.84 DA O HETATM 2855 O HOH A 509 -41.547 6.324 45.538 1.00 54.62 DA O HETATM 2856 O HOH A 510 -56.553 -0.346 17.471 1.00 43.44 DA O HETATM 2857 C1 GAL A 401 -42.567 5.445 49.031 1.00 48.25 I C HETATM 2858 O1 GAL A 401 -41.650 4.727 48.243 1.00 49.40 I O HETATM 2859 C2 GAL A 401 -43.582 4.533 49.714 1.00 47.65 I C HETATM 2860 O2 GAL A 401 -44.265 3.702 48.789 1.00 47.02 I O HETATM 2861 C3 GAL A 401 -44.634 5.394 50.407 1.00 47.38 I C HETATM 2862 O3 GAL A 401 -45.571 4.601 51.130 1.00 47.52 I O HETATM 2863 C4 GAL A 401 -43.947 6.362 51.418 1.00 45.88 I C HETATM 2864 O4 GAL A 401 -43.554 5.688 52.606 1.00 45.57 I O HETATM 2865 C5 GAL A 401 -42.719 7.042 50.765 1.00 46.85 I C HETATM 2866 O5 GAL A 401 -41.877 6.110 50.051 1.00 45.88 I O HETATM 2867 C6 GAL A 401 -41.798 7.764 51.747 1.00 48.43 I C HETATM 2868 O6 GAL A 401 -42.180 9.120 51.906 1.00 51.55 I O HETATM 2869 PA ADP A 402 -40.715 1.062 42.507 1.00 52.38 J P HETATM 2870 PB ADP A 402 -41.728 3.554 41.541 1.00 44.26 J P HETATM 2871 C5' ADP A 402 -41.662 -0.066 40.205 1.00 47.68 J C HETATM 2872 O5' ADP A 402 -41.017 -0.180 41.496 1.00 45.61 J O HETATM 2873 C4' ADP A 402 -41.605 -1.455 39.564 1.00 49.09 J C HETATM 2874 O4' ADP A 402 -42.845 -1.873 38.914 1.00 49.79 J O HETATM 2875 C3' ADP A 402 -40.492 -1.613 38.506 1.00 48.85 J C HETATM 2876 O3' ADP A 402 -39.365 -2.286 39.099 1.00 51.35 J O HETATM 2877 C2' ADP A 402 -41.132 -2.336 37.332 1.00 50.21 J C HETATM 2878 O2' ADP A 402 -40.678 -3.692 37.360 1.00 54.85 J O HETATM 2879 C1' ADP A 402 -42.638 -2.371 37.574 1.00 49.54 J C HETATM 2880 N1 ADP A 402 -45.373 -1.998 33.173 1.00 45.37 J N HETATM 2881 O1A ADP A 402 -39.289 0.865 43.018 1.00 55.97 J O1- HETATM 2882 O1B ADP A 402 -41.808 4.038 40.108 1.00 48.72 J O HETATM 2883 C2 ADP A 402 -44.457 -2.904 33.563 1.00 47.85 J C HETATM 2884 O2A ADP A 402 -41.860 1.306 43.493 1.00 53.55 J O HETATM 2885 O2B ADP A 402 -43.012 2.937 42.031 1.00 45.56 J O1- HETATM 2886 N3 ADP A 402 -43.845 -2.850 34.756 1.00 48.29 J N HETATM 2887 O3A ADP A 402 -40.665 2.345 41.557 1.00 52.41 J O HETATM 2888 O3B ADP A 402 -41.124 4.577 42.474 1.00 43.89 J O HETATM 2889 C4 ADP A 402 -44.111 -1.864 35.636 1.00 48.52 J C HETATM 2890 C5 ADP A 402 -45.105 -0.835 35.292 1.00 48.41 J C HETATM 2891 C6 ADP A 402 -45.743 -0.959 33.960 1.00 46.74 J C HETATM 2892 N6 ADP A 402 -46.665 -0.058 33.550 1.00 46.01 J N HETATM 2893 N7 ADP A 402 -45.172 0.003 36.344 1.00 46.79 J N HETATM 2894 C8 ADP A 402 -44.293 -0.471 37.278 1.00 48.46 J C HETATM 2895 N9 ADP A 402 -43.654 -1.579 36.835 1.00 50.13 J N HETATM 2896 HN61 ADP A 402 -47.094 -0.152 32.640 1.00 55.21 J H HETATM 2897 HN62 ADP A 402 -46.923 0.710 34.152 1.00 55.21 J H HETATM 2898 HO2' ADP A 402 -40.148 -3.837 38.156 1.00 65.82 J H HETATM 2899 HO3' ADP A 402 -39.670 -3.072 39.572 1.00 61.62 J H HETATM 2900 H2 ADP A 402 -44.203 -3.709 32.885 1.00 57.42 J H HETATM 2901 H8 ADP A 402 -44.128 -0.017 38.248 1.00 58.15 J H HETATM 2902 H1' ADP A 402 -42.806 -3.410 37.258 1.00 59.44 J H HETATM 2903 H2' ADP A 402 -40.882 -1.845 36.381 1.00 60.25 J H HETATM 2904 H3' ADP A 402 -40.081 -0.663 38.139 1.00 58.62 J H HETATM 2905 H4' ADP A 402 -41.406 -2.095 40.436 1.00 58.90 J H HETATM 2906 H5'1 ADP A 402 -41.147 0.667 39.581 1.00 57.22 J H HETATM 2907 H5'2 ADP A 402 -42.698 0.261 40.321 1.00 57.22 J H CONECT 2857 2858 2859 2866 CONECT 2858 2857 CONECT 2859 2857 2860 2861 CONECT 2860 2859 CONECT 2861 2859 2862 2863 CONECT 2862 2861 CONECT 2863 2861 2864 2865 CONECT 2864 2863 CONECT 2865 2863 2866 2867 CONECT 2866 2857 2865 CONECT 2867 2865 2868 CONECT 2868 2867 CONECT 2869 2872 2881 2884 2887 CONECT 2870 2882 2885 2887 2888 CONECT 2871 2873 2906 2907 2872 CONECT 2872 2869 2871 CONECT 2873 2871 2874 2875 2905 CONECT 2874 2873 2879 CONECT 2875 2873 2876 2877 2904 CONECT 2876 2875 2899 CONECT 2877 2875 2878 2879 2903 CONECT 2878 2877 2898 CONECT 2879 2874 2877 2895 2902 CONECT 2880 2883 2891 CONECT 2881 2869 CONECT 2882 2870 CONECT 2883 2880 2886 2900 CONECT 2884 2869 CONECT 2885 2870 CONECT 2886 2883 2889 CONECT 2887 2869 2870 CONECT 2888 2870 CONECT 2889 2886 2890 2895 CONECT 2890 2889 2891 2893 CONECT 2891 2890 2880 2892 CONECT 2892 2891 2896 2897 CONECT 2893 2890 2894 CONECT 2894 2893 2901 2895 CONECT 2895 2879 2889 2894 CONECT 2896 2892 CONECT 2897 2892 CONECT 2898 2878 CONECT 2899 2876 CONECT 2900 2883 CONECT 2901 2894 CONECT 2902 2879 CONECT 2903 2877 CONECT 2904 2875 CONECT 2905 2873 CONECT 2906 2871 CONECT 2907 2871 END